10 hits
XFF4834R_chr18280 | XFF4834R_chr19570711_2090547_f1_XFF4834R-XFF4834R_chr18280 | XFF4834R_chr18280 | putative outer membrane protein |
XFF4834R_chr19090 | amiC | XFF4834R_chr19090 | putative N-acetylmuramoyl-L-alanine amidase |
XFF4834R_chr24170 | XFF4834R_chr_2786303_2788060_r3_XFF4834R-XFF4834R_chr24170 | XFF4834R_chr24170 | putative N-acetylmuramoyl-L-alanine amidase |
XFF4834R_chr27260 | XFF4834R_chr29760196_3142734_r1_XFF4834R-XFF4834R_chr27260 | XFF4834R_chr27260 | putative membrane-bound lytic murein transglycosylase D |
XFF4834R_chr27830 | XFF4834R_chr30420042_3212839_r3_XFF4834R-XFF4834R_chr27830 | XFF4834R_chr27830 | putative peptidoglycan-specific endopeptidase |
XFF4834R_chr31670 | nagZ | XFF4834R_chr31670 | probable beta-N-acetylglucosaminidase |
XFF4834R_chr34560 | slt | XFF4834R_chr34560 | putative soluble lytic murein transglycosylase |
XFF4834R_chr37490 | ampD | XFF4834R_chr37490 | probable N-acetylmuramoyl-L-alanine amidase |
XFF4834R_chr41640 | XFF4834R_chr_4843538_4845694_r3_XFF4834R-XFF4834R_chr41640 | XFF4834R_chr41640 | putative lytic murein transglycosylase |
XFF4834R_plc00360 | XFF4834R_plc_0030113_0031384_r1_XFF4834R-XFF4834R_plc00360 | XFF4834R_plc00360 | putative lytic murein transglycosylase |
![]() XFF4834R_chr18270 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr18290 |
ID | XFF4834R_chr19570711_2090547_f1_XFF4834R-XFF4834R_chr18280 |
AC | XFF4834R_chr18280 |
LT | XFF4834R_chr18280 |
OR | XFF4834R_chr from 2089711 to 2090547 on strand + |
DE | putative outer membrane protein |
IP | MltA-interacting MipA |
CL | 1.7.34 Peptidoglycan (murein) turnover, recycling GO:0000270 |
EC | |
GO |
InterPro Curated |
PM | |
AN | This family consists of several bacterial MltA-interacting protein (MipA) like sequences. As well as interacting with the membrane-bound lytic transglycosylase MltA, MipA is known to bind to PBP1B, a bifunctional murein transglycosylase/transpeptidase. MipA is considered to be a structural protein mediating the assembly of MltA to PBP1B into a complex. |
CC | COG: [M] Cell wall/membrane/envelope biogenesis; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by irobene (20100825) |
MW | 29929.2 Da |
SQ | 278 aa |
........10........20........30........40........50 |
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NP_643110.1 lcl|XAC2801-XAC2801 |
1 |
278 |
S=1325 I=91 E=1.62695e-153 |
hypothetical protein |
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YP_364693.1 lcl|ompV-XCV2962 |
1 |
278 |
S=1323 I=91 E=2.47244e-153 |
outer membrane protein V |
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14 |
278 |
S=684 I=50 E=6.83481e-76 |
putative outer membrane protein |
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1 |
44 |
S=203 I=89 E=4.42073e-17 |
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140 |
179 |
S=200 I=95 E=8.95779e-17 |
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45 |
132 |
S=146 I=38 E=3.53421e-10 |
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116 |
174 |
S=129 I=46 E=3.88346e-08 |
Access unfiltered results
![]() |
Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
0 hits |
![]() |
Swiss-Prot ncbi-blastp |
0 hits |
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Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
0 hits |
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HAMAP scan |
0 hits |
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IprScan |
0 hits |
Miscellaneous analyses
![]() XFF4834R_chr19080 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr19100 |
ID | amiC |
AC | XFF4834R_chr19090 |
LT | XFF4834R_chr19090 |
OR | XFF4834R_chr from 2185780 to 2186928 on strand + |
DE | putative N-acetylmuramoyl-L-alanine amidase |
IP | Cell wall hydrolase/autolysin, catalytic |
CL | 1.7.34 Peptidoglycan (murein) turnover, recycling GO:0000270 |
EC | |
GO |
InterPro Biological Process: peptidoglycan catabolic process (GO:0009253) Molecular Function: N-acetylmuramoyl-L-alanine amidase activity (GO:0008745) Curated |
PM | |
AN | |
CC | COG: [M] Cell wall/membrane/envelope biogenesis; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by irobene (20100509) |
MW | 40637.7 Da |
SQ | 382 aa |
........10........20........30........40........50 |
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XFF4834R_chr24170 lcl|XFF4834R_chr_2786303_2788060_r3_XFF4834R-XFF4834R_chr24170 |
137 |
379 |
S=423 I=42 E=1.16823e-44 |
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XFF4834R_chr24170 lcl|XFF4834R_chr_2786303_2788060_r3_XFF4834R-XFF4834R_chr24170 |
137 |
379 |
S=423 I=42 E=1.16823e-44 |
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NP_642108.1 lcl|amiC-XAC1780 |
1 |
382 |
S=1383 I=73 E=2.01763e-160 |
N-acetylmuramoyl-L-alanine amidase |
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NP_637130.1 lcl|amiC-XCC1763 |
1 |
382 |
S=1348 I=72 E=3.76721e-156 |
N-acetylmuramoyl-L-alanine amidase |
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YP_363543.1 lcl|amiC-XCV1812 |
1 |
382 |
S=1333 I=72 E=2.49648e-154 |
N-acetylmuramoyl-L-alanine amidase precursor |
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18 |
379 |
S=1065 I=61 E=7.6165e-122 |
probable n-acetylmuramoyl-l-alanine amidase precursor protein |
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NP_637654.1 lcl|amiC-XCC2299 |
137 |
375 |
S=444 I=43 E=1.36382e-46 |
N-acetylmuramoyl-L-alanine amidase |
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YP_364334.1 lcl|amiC-XCV2603 |
137 |
379 |
S=422 I=42 E=5.78883e-44 |
N-acetylmuramoyl-L-alanine amidase precursor |
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NP_642722.1 lcl|amiC-XAC2406 |
137 |
379 |
S=421 I=42 E=6.95196e-44 |
N-acetylmuramoyl-L-alanine amidase |
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149 |
379 |
S=418 I=40 E=1.69173e-43 |
hypothetical n-acetylmuramoyl-l-alanine amidase protein |
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150 |
379 |
S=474 I=48 E=1.03277e-48 |
Putative acetyl-muramoyl-alanine amidase |
Pubmed 15658985 |
|
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153 |
378 |
S=447 I=43 E=2.31772e-45 |
Probable N-acetylmuramoyl-L-alanine amidase amiA EC=3.5.1.28 ; Cell wall biogenesis/degradation Hydrolase Secreted Signal |
Pubmed 8300522 |
|
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153 |
379 |
S=441 I=40 E=1.04743e-44 |
N-acetylmuramoyl-L-alanine amidase amiB EC=3.5.1.28 ; Cell wall biogenesis/degradation Hydrolase Secreted Signal |
Pubmed 7511774 |
|
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153 |
378 |
S=440 I=42 E=1.45886e-44 |
Probable N-acetylmuramoyl-L-alanine amidase amiA EC=3.5.1.28 ; Cell wall biogenesis/degradation Hydrolase Secreted Signal |
Pubmed 8349542 |
|
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153 |
379 |
S=431 I=41 E=1.53592e-43 |
N-acetylmuramoyl-L-alanine amidase amiB EC=3.5.1.28 ; Cell wall biogenesis/degradation Hydrolase Secreted Signal |
Pubmed 2676972 |
|
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41 |
375 |
S=427 I=34 E=4.72964e-43 |
Putative N-acetylmuramoyl-L-alanine amidase-precursor AmiC |
Pubmed 10844690 |
|
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41 |
375 |
S=423 I=33 E=1.52132e-42 |
AmiC |
Pubmed 10844690 |
|
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41 |
375 |
S=416 I=34 E=1.21174e-41 |
N-acetylmuramoyl-L-alanine amidase amiC EC=3.5.1.28 ; Cell wall biogenesis/degradation Hydrolase Secreted Signal |
Pubmed 17038831 |
|
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86 |
379 |
S=355 I=34 E=3.06214e-34 |
Predicted N-acetylmuramoyl-L-alanine amidase |
Pubmed 10988064 |
|
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23 |
229 |
S=188 I=30 E=4.907e-14 |
CwlV |
Pubmed 10628856 |
|
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148 |
376 |
S=511 I=45 E=2.14209e-53 |
N-acetylmuramoyl-L-alanine amidase amiC EC=3.5.1.28 ; Cell wall biogenesis/degradation Hydrolase Secreted Signal |
||
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148 |
376 |
S=511 I=45 E=2.14209e-53 |
N-acetylmuramoyl-L-alanine amidase amiC EC=3.5.1.28 ; Cell wall biogenesis/degradation Hydrolase Secreted Signal |
||
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153 |
378 |
S=447 I=43 E=1.59581e-45 |
Probable N-acetylmuramoyl-L-alanine amidase amiA EC=3.5.1.28 ; Cell wall biogenesis/degradation Hydrolase Secreted Signal |
||
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153 |
379 |
S=441 I=40 E=7.21185e-45 |
N-acetylmuramoyl-L-alanine amidase amiB EC=3.5.1.28 ; Cell wall biogenesis/degradation Hydrolase Secreted Signal |
||
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153 |
378 |
S=440 I=42 E=1.00446e-44 |
Probable N-acetylmuramoyl-L-alanine amidase amiA EC=3.5.1.28 ; Cell wall biogenesis/degradation Hydrolase Secreted Signal |
||
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259 |
335 |
S=162 I=49 E=3.89261e-12 |
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190 |
263 |
S=140 I=46 E=1.933e-09 |
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152 |
234 |
S=112 I=37 E=5.03106e-06 |
Access unfiltered results
![]() |
Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
22 hits |
![]() |
Swiss-Prot ncbi-blastp |
18 hits |
![]() |
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
1 hits |
![]() |
HAMAP scan |
0 hits |
![]() |
IprScan |
0 hits |
Miscellaneous analyses
![]() XFF4834R_chr24160 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr24180 |
ID | XFF4834R_chr_2786303_2788060_r3_XFF4834R-XFF4834R_chr24170 |
AC | XFF4834R_chr24170 |
LT | XFF4834R_chr24170 |
OR | XFF4834R_chr from 2786303 to 2788036 on strand - |
DE | putative N-acetylmuramoyl-L-alanine amidase |
IP | Cell wall hydrolase/autolysin, catalytic; Localisation of periplasmic protein complexes |
CL | 1.7.34 Peptidoglycan (murein) turnover, recycling GO:0000270 |
EC | |
GO |
InterPro Biological Process: peptidoglycan catabolic process (GO:0009253) Molecular Function: N-acetylmuramoyl-L-alanine amidase activity (GO:0008745) Curated |
PM | |
AN | Zn-dependent peptidases AMIN : This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localises to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localisation of periplasmic protein complexes [1]. |
CC | COG: [M] Cell wall/membrane/envelope biogenesis; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by irobene (20100525) |
MW | 57970 Da |
SQ | 577 aa |
........10........20........30........40........50 |
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XFF4834R_chr19090 lcl|amiC-XFF4834R_chr19090 |
315 |
552 |
S=437 I=42 E=3.52288e-46 |
N-acetylmuramoyl-L-alanine amidase |
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NP_637654.1 lcl|amiC-XCC2299 |
303 |
577 |
S=1335 I=92 E=2.34527e-154 |
N-acetylmuramoyl-L-alanine amidase |
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NP_637654.1 lcl|amiC-XCC2299 |
1 |
138 |
S=541 I=81 E=3.4965e-58 |
N-acetylmuramoyl-L-alanine amidase |
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NP_642722.1 lcl|amiC-XAC2406 |
303 |
577 |
S=1316 I=99 E=4.16272e-152 |
N-acetylmuramoyl-L-alanine amidase |
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NP_642722.1 lcl|amiC-XAC2406 |
1 |
138 |
S=684 I=97 E=1.67556e-75 |
N-acetylmuramoyl-L-alanine amidase |
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YP_364334.1 lcl|amiC-XCV2603 |
246 |
577 |
S=1308 I=84 E=4.12314e-151 |
N-acetylmuramoyl-L-alanine amidase precursor |
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YP_364334.1 lcl|amiC-XCV2603 |
7 |
138 |
S=650 I=96 E=1.91996e-71 |
N-acetylmuramoyl-L-alanine amidase precursor |
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309 |
577 |
S=1131 I=83 E=1.04795e-129 |
hypothetical n-acetylmuramoyl-l-alanine amidase protein |
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53 |
138 |
S=298 I=63 E=9.14095e-29 |
hypothetical n-acetylmuramoyl-l-alanine amidase protein |
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326 |
552 |
S=479 I=44 E=1.17816e-50 |
probable n-acetylmuramoyl-l-alanine amidase precursor protein |
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YP_363543.1 lcl|amiC-XCV1812 |
325 |
552 |
S=443 I=43 E=2.78368e-46 |
N-acetylmuramoyl-L-alanine amidase precursor |
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NP_642108.1 lcl|amiC-XAC1780 |
313 |
552 |
S=442 I=42 E=3.81007e-46 |
N-acetylmuramoyl-L-alanine amidase |
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NP_637130.1 lcl|amiC-XCC1763 |
313 |
552 |
S=434 I=41 E=2.85506e-45 |
N-acetylmuramoyl-L-alanine amidase |
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IPR002508 [G3DSA:3.40.630.40] | 327 |
548 |
Cell wall hydrolase/autolysin, catalytic |
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IPR002508 [PF01520] | 330 |
545 |
Cell wall hydrolase/autolysin, catalytic |
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IPR021731 [PF11741] | 32 |
118 |
Localisation of periplasmic protein complexes |
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IPR002508 [SM00646] | 390 |
545 |
Cell wall hydrolase/autolysin, catalytic |
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[seg] | 139 |
158 |
- |
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[seg] | 163 |
243 |
- |
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[seg] | 257 |
270 |
- |
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[seg] | 277 |
302 |
- |
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[SignalP-NN(euk)] | 1 |
29 |
- |
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[SSF53187] | 327 |
551 |
- |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr27250 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr27270 |
ID | XFF4834R_chr29760196_3142734_r1_XFF4834R-XFF4834R_chr27260 |
AC | XFF4834R_chr27260 |
LT | XFF4834R_chr27260 |
OR | XFF4834R_chr from 3141196 to 3142779 on strand - |
DE | putative membrane-bound lytic murein transglycosylase D |
IP | Lytic transglycosylase-like, catalytic; Peptidoglycan-binding lysin domain |
CL | 1.7.34 Peptidoglycan (murein) turnover, recycling GO:0000270 |
EC | |
GO |
InterPro Biological Process: cell wall macromolecule catabolic process (GO:0016998) Curated |
PM | |
AN | start change |
CC | COG: [M] Cell wall/membrane/envelope biogenesis; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by irobene (20100619) |
MW | 57007.2 Da |
SQ | 527 aa |
........10........20........30........40........50 |
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XFF4834R_chr24420 lcl|XFF4834R_chr26690099_2818082_r2_XFF4834R-XFF4834R_chr24420 |
201 |
290 |
S=123 I=38 E=3.7243e-08 |
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XFF4834R_chr10670 lcl|mltD-XFF4834R_chr10670 |
189 |
347 |
S=104 I=29 E=7.534e-06 |
predicted membrane-bound lytic murein transglycosylase D |
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YP_364612.1 lcl|XCV2881 |
1 |
527 |
S=2499 I=90 E=0 |
lytic mureine transglycosylase precursor |
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NP_643038.1 lcl|dniR-XAC2729 |
58 |
527 |
S=2276 I=92 E=0 |
membrane-bound lytic murein transglycosylase D precursor |
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NP_637905.1 lcl|dniR-XCC2557 |
56 |
527 |
S=2130 I=85 E=0 |
membrane-bound lytic murein transglycosylase D precursor |
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1 |
527 |
S=1845 I=66 E=0 |
putative membrane-bound lytic murein transglycosylase d precursor (murein hydrolase d) protein |
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185 |
290 |
S=133 I=38 E=8.34814e-09 |
hypothetical soluble lytic murein transglycosylase precursor protein |
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YP_364366.1 lcl|XCV2635 |
201 |
290 |
S=123 I=38 E=1.33567e-07 |
putative soluble lytic murein transglycosylase precursor |
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NP_642773.1 lcl|yjbJ-XAC2458 |
201 |
290 |
S=123 I=38 E=1.52228e-07 |
soluble lytic murein transglycosylase |
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NP_637679.1 lcl|yjbJ-XCC2325 |
201 |
290 |
S=121 I=38 E=2.2933e-07 |
soluble lytic murein transglycosylase |
![]() |
222 |
300 |
S=107 I=35 E=1.34512e-05 |
probable membrane-bound murein hydrolase d precursor protein |
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NP_641425.1 lcl|dniR-XAC1086 |
189 |
345 |
S=106 I=29 E=1.54648e-05 |
murein hydrolase D |
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YP_362817.1 lcl|mltD-XCV1086 |
189 |
347 |
S=105 I=28 E=2.09832e-05 |
membrane-bound murein hydrolase D |
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[G3DSA:1.10.530.10] | 189 |
351 |
- |
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[G3DSA:3.10.350.10] | 475 |
525 |
- |
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[PTHR21666:SF10] | 188 |
293 |
- |
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[PTHR21666] | 188 |
293 |
- |
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IPR008258 [PF01464] | 198 |
302 |
Lytic transglycosylase-like, catalytic |
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IPR018392 [PF01476] | 479 |
522 |
Peptidoglycan-binding lysin domain |
![]() |
IPR002482 [SM00257] | 478 |
523 |
Peptidoglycan-binding Lysin subgroup |
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[seg] | 37 |
47 |
- |
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[seg] | 106 |
120 |
- |
![]() |
[seg] | 256 |
265 |
- |
![]() |
[seg] | 465 |
476 |
- |
![]() |
[SignalP-NN(euk)] | 1 |
28 |
- |
![]() |
[SSF53955] | 187 |
353 |
- |
![]() |
[SSF54106] | 475 |
522 |
- |
Access unfiltered results
![]() |
Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
7 hits |
![]() |
Swiss-Prot ncbi-blastp |
4 hits |
![]() |
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
3 hits |
![]() |
HAMAP scan |
0 hits |
![]() |
IprScan |
14 hits |
Miscellaneous analyses
![]() XFF4834R_chr27820 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr27840 |
ID | XFF4834R_chr30420042_3212839_r3_XFF4834R-XFF4834R_chr27830 |
AC | XFF4834R_chr27830 |
LT | XFF4834R_chr27830 |
OR | XFF4834R_chr from 3212042 to 3212821 on strand - |
DE | putative peptidoglycan-specific endopeptidase |
IP | Peptidase M23B; Peptidase M23; Peptidoglycan-binding lysin domain |
CL | 1.7.34 Peptidoglycan (murein) turnover, recycling GO:0000270 |
EC | |
GO |
InterPro Biological Process: cell wall macromolecule catabolic process (GO:0016998) Biological Process: proteolysis (GO:0006508) Molecular Function: metalloendopeptidase activity (GO:0004222) Curated |
PM | |
AN | start change |
CC | COG: [M] Cell wall/membrane/envelope biogenesis; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by irobene (20100622) |
MW | 26677.2 Da |
SQ | 259 aa |
........10........20........30........40........50 |
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XFF4834R_chr00250 lcl|envC-XFF4834R_chr00250 |
160 |
259 |
S=186 I=41 E=3.5301e-16 |
protease with a role in cell division |
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XFF4834R_chr07910 lcl|XFF4834R_chr08370943_0914884_f2_XFF4834R-XFF4834R_chr07910 |
160 |
256 |
S=161 I=37 E=4.30317e-13 |
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XFF4834R_chr37850 lcl|XFF4834R_chr40950456_4376874_f1_XFF4834R-XFF4834R_chr37850 |
160 |
253 |
S=136 I=35 E=4.44474e-10 |
![]() |
XFF4834R_chr23660 lcl|XFF4834R_chr25860280_2737122_f1_XFF4834R-XFF4834R_chr23660 |
161 |
258 |
S=107 I=32 E=1.38928e-06 |
![]() |
NP_642059.1 lcl|nlpD-XAC1728 |
1 |
259 |
S=923 I=71 E=7.1086e-105 |
lipoprotein |
![]() |
YP_363492.1 lcl|nlpD-XCV1761 |
1 |
259 |
S=914 I=71 E=8.30956e-104 |
outer membrane lipoprotein |
![]() |
NP_637079.1 lcl|nlpD-XCC1709 |
1 |
259 |
S=867 I=68 E=4.29946e-98 |
lipoprotein |
![]() |
7 |
259 |
S=686 I=55 E=3.3358e-76 |
putative outer membrane lipoprotein precursor |
![]() |
161 |
259 |
S=197 I=42 E=6.05345e-17 |
putative peptidase protein |
![]() |
NP_635417.1 lcl|XCC0022 |
160 |
259 |
S=188 I=41 E=7.52148e-16 |
hypothetical protein |
![]() |
YP_361756.1 lcl|XCV0025 |
160 |
259 |
S=185 I=41 E=1.86251e-15 |
putative peptidase |
![]() |
NP_640380.1 lcl|XAC0024-XAC0024 |
160 |
259 |
S=182 I=40 E=3.9422e-15 |
hypothetical protein |
![]() |
NP_636124.1 lcl|XCC0733 |
160 |
256 |
S=163 I=37 E=9.49403e-13 |
peptidase |
![]() |
NP_641139.1 lcl|XAC0787-XAC0787 |
160 |
256 |
S=161 I=37 E=1.43027e-12 |
peptidase |
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YP_362569.1 lcl|XCV0838 |
160 |
256 |
S=161 I=37 E=1.48103e-12 |
membrane-bound metalloendopeptidase |
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160 |
256 |
S=149 I=35 E=4.287e-11 |
putative membrane-bound metalloendopeptidase protein |
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YP_365742.1 lcl|XCV4011 |
160 |
253 |
S=136 I=35 E=1.66911e-09 |
membrane-bound metalloendopeptidase |
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NP_644199.1 lcl|XAC3898-XAC3898 |
160 |
253 |
S=136 I=35 E=1.69847e-09 |
hypothetical protein |
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NP_639182.1 lcl|XCC3842 |
160 |
253 |
S=135 I=35 E=1.98708e-09 |
hypothetical protein |
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160 |
252 |
S=117 I=33 E=3.4359e-07 |
hypothetical membrane-bound metalloendopeptidase protein |
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YP_364291.1 lcl|XCV2560 |
161 |
258 |
S=110 I=32 E=2.50821e-06 |
metalloendopeptidase precursor |
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NP_642677.1 lcl|XAC2361-XAC2361 |
161 |
258 |
S=109 I=32 E=2.83383e-06 |
peptidase |
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[G3DSA:3.10.350.10] | 56 |
105 |
- |
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IPR002886 [PTHR21666:SF7] | 61 |
253 |
Peptidase M23B |
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[PTHR21666] | 61 |
253 |
- |
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IPR016047 [PF01551] | 159 |
252 |
Peptidase M23 |
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IPR018392 [PF01476] | 61 |
101 |
Peptidoglycan-binding lysin domain |
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IPR002482 [SM00257] | 59 |
103 |
Peptidoglycan-binding Lysin subgroup |
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[PS51257] | 1 |
25 |
- |
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[seg] | 30 |
58 |
- |
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[seg] | 104 |
119 |
- |
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[seg] | 121 |
134 |
- |
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[seg] | 146 |
158 |
- |
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[SignalP-NN(euk)] | 1 |
27 |
- |
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[tmhmm] | 12 |
31 |
- |
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IPR011055 [SSF51261] | 56 |
256 |
Duplicated hybrid motif |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr31660 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr31680 |
ID | nagZ |
AC | XFF4834R_chr31670 |
LT | XFF4834R_chr31670 |
OR | XFF4834R_chr from 3635869 to 3636873 on strand - |
DE | probable beta-N-acetylglucosaminidase |
IP | Glycoside hydrolase, catalytic core |
CL | 1.7.34 Peptidoglycan (murein) turnover, recycling GO:0000270 |
EC | |
GO |
InterPro Biological Process: carbohydrate metabolic process (GO:0005975) hydrolyzing O-glycosyl compounds (GO:0004553) Curated |
PM | |
AN | peptidoglycan recycling |
CC | COG: [G] Carbohydrate transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by elauber (20100719) |
MW | 34954.3 Da |
SQ | 334 aa |
........10........20........30........40........50 |
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XFF4834R_chr37580 lcl|bglX-XFF4834R_chr37580 |
107 |
247 |
S=133 I=32 E=1.49561e-09 |
beta-D-glucoside glucohydrolase, periplasmic |
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XFF4834R_chr41060 lcl|XFF4834R_chr_4767686_4770391_f2_XFF4834R-XFF4834R_chr41060 |
117 |
247 |
S=95 I=32 E=5.37012e-05 |
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NP_641669.1 lcl|nagZ-XAC1334 |
1 |
334 |
S=1441 I=89 E=1.57842e-167 |
beta-hexosaminidase |
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YP_363117.1 lcl|XCV1386 |
1 |
334 |
S=1424 I=88 E=1.66042e-165 |
beta-hexosaminidase |
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NP_636657.1 lcl|nagZ-XCC1283 |
1 |
334 |
S=1313 I=82 E=4.80001e-152 |
beta-hexosaminidase |
![]() |
1 |
323 |
S=1099 I=73 E=4.61572e-126 |
probable beta-n-acetylhexosaminidase protein |
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YP_365719.1 lcl|bglX-XCV3988 |
107 |
247 |
S=133 I=32 E=5.20558e-09 |
beta-glucosidase |
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NP_644175.1 lcl|bglX-XAC3869 |
107 |
247 |
S=129 I=32 E=1.46914e-08 |
beta-glucosidase |
![]() |
107 |
247 |
S=123 I=32 E=7.70015e-08 |
probable beta-glucosidase protein |
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NP_639159.1 lcl|bglX-XCC3814 |
107 |
247 |
S=122 I=32 E=1.18042e-07 |
beta-glucosidase |
![]() |
NP_636624.1 lcl|bglX-XCC1250 |
112 |
247 |
S=105 I=30 E=1.24174e-05 |
beta-glucosidase |
![]() |
NP_644530.1 lcl|XAC4231-XAC4231 |
117 |
247 |
S=104 I=33 E=1.61297e-05 |
glucan 1,4-beta-glucosidase |
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YP_366068.1 lcl|XCV4337 |
117 |
247 |
S=103 I=32 E=2.28606e-05 |
beta-glucosidase precursor |
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2 |
279 |
S=606 I=46 E=1.07753e-64 |
Beta-hexosaminidase EC=3.2.1.52 ; Cell cycle division shape wall biogenesis/degradation Cytoplasm Glycosidase Hydrolase Peptidoglycan synthesis |
Pubmed 8969206 |
|
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2 |
291 |
S=605 I=45 E=1.42428e-64 |
Putative beta-hexosaminidase ; Glycosidase Hydrolase |
Pubmed 20091296 |
|
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6 |
290 |
S=552 I=39 E=3.79573e-58 |
Beta-N-acetylhexosaminidase. Glycosyl Hydrolase family 3 EC=3.2.1.52 Putative N-acetyl-glucosaminidase ; Glycosidase |
Pubmed 12754233 |
|
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2 |
279 |
S=537 I=44 E=2.07635e-56 |
N-acetylhexosaminidase EC=3.2.1.52 ; Glycosidase Hydrolase |
Pubmed 18671744 |
|
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2 |
292 |
S=432 I=33 E=1.20673e-43 |
Putative hydrolase ; Glycosidase |
Pubmed 14993314 |
|
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1 |
334 |
S=1441 I=89 E=4.48726e-166 |
Beta-hexosaminidase EC=3.2.1.52 ; Cell cycle division shape wall biogenesis/degradation Cytoplasm Glycosidase Hydrolase Peptidoglycan synthesis |
||
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1 |
334 |
S=1425 I=88 E=4.40233e-164 |
Beta-hexosaminidase EC=3.2.1.52 ; Cell cycle division shape wall biogenesis/degradation Cytoplasm Glycosidase Hydrolase Peptidoglycan synthesis |
||
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1 |
334 |
S=1417 I=87 E=3.29887e-163 |
Beta-hexosaminidase EC=3.2.1.52 ; Cell cycle division shape wall biogenesis/degradation Cytoplasm Glycosidase Hydrolase Peptidoglycan synthesis |
||
![]() |
1 |
334 |
S=1410 I=87 E=2.30545e-162 |
Beta-hexosaminidase EC=3.2.1.52 ; Cell cycle division shape wall biogenesis/degradation Cytoplasm Glycosidase Hydrolase Peptidoglycan synthesis |
||
![]() |
1 |
334 |
S=1313 I=82 E=1.36458e-150 |
Beta-hexosaminidase EC=3.2.1.52 ; Cell cycle division shape wall biogenesis/degradation Cytoplasm Glycosidase Hydrolase Peptidoglycan synthesis |
||
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IPR001764 [G3DSA:3.20.20.300] | 1 |
278 |
Glycoside hydrolase, family 3, N-terminal |
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[MF_00364] | 1 |
334 |
- |
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IPR001764 [PF00933] | 54 |
276 |
Glycoside hydrolase, family 3, N-terminal |
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IPR019800 [PS00775] | 233 |
250 |
Glycoside hydrolase, family 3, active site |
![]() |
[seg] | 84 |
105 |
- |
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[seg] | 298 |
310 |
- |
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109 |
291 |
S=231 I=31 E=1.61793e-20 |
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33 |
276 |
S=203 I=33 E=4.32262e-17 |
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209 |
253 |
S=138 I=50 E=3.67019e-09 |
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106 |
150 |
S=117 I=47 E=1.07079e-06 |
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153 |
210 |
S=116 I=48 E=1.42777e-06 |
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2 |
70 |
S=105 I=41 E=3.26598e-05 |
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1 |
25 |
S=104 I=88 E=4.02614e-05 |
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206 |
279 |
S=103 I=36 E=5.96049e-05 |
![]() |
IPR017853 [SSF51445] | 1 |
278 |
Glycoside hydrolase, catalytic core |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr34550 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr34570 |
ID | slt |
AC | XFF4834R_chr34560 |
LT | XFF4834R_chr34560 |
OR | XFF4834R_chr from 4009150 to 4011123 on strand + |
DE | putative soluble lytic murein transglycosylase |
IP | Lytic transglycosylase-like, catalytic; Lytic transglycosylase, superhelical U-shaped and linker domain |
CL | 1.7.34 Peptidoglycan (murein) turnover, recycling GO:0000270 |
EC | |
GO |
InterPro Cellular Component: periplasmic space (GO:0042597) hydrolyzing O-glycosyl compounds (GO:0004553) Curated |
PM | |
AN | Also CL 1.2.3 Proteins/peptides/glycopeptides (CL 1.6.7 Peptidoglycan (murein) is for biosynthesis) |
CC | COG: [M] Cell wall/membrane/envelope biogenesis; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by irobene (20100811) |
MW | 72142.7 Da |
SQ | 657 aa |
........10........20........30........40........50 |
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XFF4834R_chr24420 lcl|XFF4834R_chr26690099_2818082_r2_XFF4834R-XFF4834R_chr24420 |
449 |
598 |
S=126 I=31 E=2.1353e-08 |
![]() |
NP_643868.1 lcl|slt-XAC3561 |
1 |
657 |
S=3140 I=92 E=0 |
soluble lytic murein transglycosylase |
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YP_365417.1 lcl|slt-XCV3686 |
1 |
657 |
S=3127 I=92 E=0 |
soluble lytic murein transglycosylase precursor |
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NP_638752.1 lcl|slt-XCC3406 |
1 |
657 |
S=2935 I=86 E=0 |
soluble lytic murein transglycosylase |
![]() |
18 |
645 |
S=2264 I=69 E=0 |
probable soluble lytic murein transglycosylase precursor protein |
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NP_642773.1 lcl|yjbJ-XAC2458 |
449 |
598 |
S=124 I=32 E=1.20972e-07 |
soluble lytic murein transglycosylase |
![]() |
YP_364366.1 lcl|XCV2635 |
449 |
598 |
S=124 I=32 E=1.31993e-07 |
putative soluble lytic murein transglycosylase precursor |
![]() |
NP_637679.1 lcl|yjbJ-XCC2325 |
449 |
598 |
S=120 I=31 E=3.82389e-07 |
soluble lytic murein transglycosylase |
![]() |
474 |
598 |
S=109 I=32 E=9.13677e-06 |
hypothetical soluble lytic murein transglycosylase precursor protein |
![]() |
463 |
594 |
S=106 I=31 E=2.32246e-05 |
probable lytic transglycosylase protein |
![]() |
7 |
630 |
S=559 I=30 E=1.01522e-58 |
Putative soluble lytic transglycosylase |
Pubmed 20091296 |
|
![]() |
6 |
624 |
S=478 I=27 E=6.86002e-49 |
Soluble lytic murein transglycosylase EC=4.2.2.n1 ; Cell wall biogenesis/degradation Disulfide bond Lyase Periplasm Signal |
Pubmed 1938883 |
|
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18 |
632 |
S=447 I=28 E=4.90894e-45 |
Soluble lytic murein transglycosylase |
Pubmed 15305924 |
|
![]() |
482 |
613 |
S=156 I=36 E=6.87586e-10 |
Membrane-bound lytic murein transglycosylase C EC=3.2.1.- ; Glycosidase Hydrolase |
Pubmed 18459973 |
|
![]() |
487 |
581 |
S=155 I=37 E=1.00034e-09 |
Putative lytic transglycosylase ; Signal |
Pubmed 12820036 |
|
![]() |
6 |
624 |
S=478 I=27 E=4.67039e-49 |
Soluble lytic murein transglycosylase EC=4.2.2.n1 ; Cell wall biogenesis/degradation Disulfide bond Lyase Periplasm Signal |
||
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6 |
624 |
S=478 I=27 E=4.67039e-49 |
Soluble lytic murein transglycosylase EC=4.2.2.n1 ; Cell wall biogenesis/degradation Disulfide bond Lyase Periplasm Signal |
||
![]() |
6 |
617 |
S=465 I=28 E=1.71072e-47 |
Soluble lytic murein transglycosylase EC=4.2.2.n1 ; Cell wall biogenesis/degradation Disulfide bond Lyase Periplasm Signal |
||
![]() |
329 |
617 |
S=260 I=30 E=1.40729e-22 |
Putative soluble lytic murein transglycosylase EC=4.2.2.n1 ; Cell wall biogenesis/degradation Lyase Periplasm Signal |
||
![]() |
475 |
599 |
S=176 I=36 E=1.91016e-12 |
Putative murein lytic transglycosylase yjbJ EC=4.-.-.- ; Lyase |
||
![]() |
IPR008939 [G3DSA:1.25.20.10] | 25 |
381 |
Lytic transglycosylase, superhelical U-shaped |
![]() |
[G3DSA:1.10.530.10] | 467 |
637 |
- |
![]() |
[PTHR21666:SF10] | 462 |
580 |
- |
![]() |
[PTHR21666] | 462 |
580 |
- |
![]() |
IPR008258 [PF01464] | 478 |
589 |
Lytic transglycosylase-like, catalytic |
![]() |
[seg] | 183 |
194 |
- |
![]() |
[seg] | 204 |
218 |
- |
![]() |
[seg] | 352 |
364 |
- |
![]() |
[SignalP-NN(euk)] | 1 |
24 |
- |
![]() |
[tmhmm] | 7 |
24 |
- |
![]() |
35 |
471 |
S=531 I=34 E=9.12206e-57 |
![]() |
1 |
51 |
S=256 I=98 E=2.17839e-23 |
![]() |
618 |
657 |
S=211 I=100 E=5.32514e-18 |
![]() |
24 |
145 |
S=133 I=32 E=1.76037e-08 |
![]() |
472 |
498 |
S=130 I=93 E=3.72601e-08 |
![]() |
499 |
584 |
S=118 I=38 E=1.21856e-06 |
![]() |
240 |
345 |
S=116 I=33 E=2.09223e-06 |
![]() |
51 |
136 |
S=112 I=28 E=5.85352e-06 |
![]() |
486 |
522 |
S=104 I=57 E=5.4546e-05 |
![]() |
582 |
634 |
S=104 I=36 E=5.50236e-05 |
![]() |
IPR016026 [SSF48435] | 25 |
471 |
Lytic transglycosylase, superhelical U-shaped and linker domain |
![]() |
[SSF53955] | 472 |
637 |
- |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr_4592 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr37500 |
ID | ampD |
AC | XFF4834R_chr37490 |
LT | XFF4834R_chr37490 |
OR | XFF4834R_chr from 4334444 to 4335250 on strand - |
DE | probable N-acetylmuramoyl-L-alanine amidase |
IP | N-acetylmuramoyl-L-alanine amidase, family 2 |
CL | 1.7.34 Peptidoglycan (murein) turnover, recycling GO:0000270 |
EC | |
GO |
InterPro Biological Process: peptidoglycan catabolic process (GO:0009253) Molecular Function: N-acetylmuramoyl-L-alanine amidase activity (GO:0008745) Curated |
PM | |
AN | |
CC | COG: [V] Defense mechanisms; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by poussier (20100712) |
MW | 29157.2 Da |
SQ | 268 aa |
........10........20........30........40........50 |
![]() |
YP_365709.1 lcl|ampD-XCV3978 |
1 |
268 |
S=1240 I=93 E=3.10745e-143 |
N-acetylmuramoyl-L-alanine amidase |
![]() |
NP_644166.1 lcl|XAC3860-XAC3860 |
1 |
267 |
S=1205 I=91 E=5.22569e-139 |
N-acetylmuramoyl-L-alanine amidase |
![]() |
NP_639150.1 lcl|XCC3805 |
12 |
248 |
S=958 I=84 E=4.02742e-109 |
N-acetylmuramoyl-L-alanine amidase |
![]() |
25 |
249 |
S=817 I=73 E=4.72707e-92 |
probable n-acetylmuramoyl-l-alanine amidase precursor protein |
![]() |
40 |
250 |
S=226 I=33 E=8.32348e-19 |
BimB N-acetylmuramoyl-L-alanine amidase domain protein |
Pubmed 16267310 |
|
![]() |
78 |
187 |
S=201 I=41 E=9.71346e-16 |
N-acetylmuramyl-L-alanine amidase |
Pubmed 9390420 |
|
![]() |
75 |
195 |
S=180 I=40 E=3.01227e-13 |
N-acetyl-anhydromuramyl-L-alanine amidase |
Pubmed 14766547 |
|
![]() |
78 |
181 |
S=175 I=38 E=1.20489e-12 |
N-acetyl-anhydromuramyl-L-alanine amidase variant 3 |
Pubmed 11557489 |
|
![]() |
78 |
181 |
S=175 I=38 E=1.36132e-12 |
N-acetyl-anhydromuramyl-L-alanine amidase |
Pubmed 11557489 |
|
![]() |
49 |
192 |
S=238 I=39 E=2.17726e-20 |
N-acetylmuramoyl-L-alanine amidase AmiD EC=3.5.1.28 ; Cell membrane outer wall biogenesis/degradation Hydrolase Lipoprotein Metal-binding Palmita |
||
![]() |
78 |
180 |
S=181 I=38 E=1.66639e-13 |
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD EC=3.5.1.28 ; Cell wall biogenesis/degradation Cytoplasm Hydrolase Metal-binding Zinc |
||
![]() |
79 |
181 |
S=171 I=38 E=2.90904e-12 |
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD EC=3.5.1.28 ; Cell wall biogenesis/degradation Cytoplasm Hydrolase Metal-binding Zinc |
||
![]() |
78 |
181 |
S=169 I=38 E=4.57771e-12 |
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD EC=3.5.1.28 ; Cell wall biogenesis/degradation Cytoplasm Hydrolase Metal-binding Zinc |
||
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