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Protein

N-acetylmuramoyl-L-alanine amidase XlyA

Gene

xlyA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation.

Catalytic activityi

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation, Competence, Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU12810-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylmuramoyl-L-alanine amidase XlyA (EC:3.5.1.28)
Alternative name(s):
Autolysin
Cell wall hydrolase
Gene namesi
Name:xlyA
Ordered Locus Names:BSU12810
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 44Sequence analysisAdd BLAST44
ChainiPRO_000000645745 – 297N-acetylmuramoyl-L-alanine amidase XlyAAdd BLAST253

Proteomic databases

PaxDbiP39800.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007101.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Beta strandi25 – 30Combined sources6
Helixi40 – 47Combined sources8
Beta strandi57 – 60Combined sources4
Beta strandi65 – 67Combined sources3
Beta strandi78 – 80Combined sources3
Helixi84 – 87Combined sources4
Beta strandi88 – 94Combined sources7
Helixi102 – 119Combined sources18
Helixi124 – 126Combined sources3
Beta strandi127 – 129Combined sources3
Helixi130 – 134Combined sources5
Turni140 – 142Combined sources3
Helixi143 – 145Combined sources3
Helixi146 – 151Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HMBX-ray2.70A/B/C1-154[»]
3RDRX-ray2.20A1-154[»]
ProteinModelPortaliP39800.
SMRiP39800.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini159 – 203LysMPROSITE-ProRule annotationAdd BLAST45

Sequence similaritiesi

Contains 1 LysM domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108VPC. Bacteria.
COG1388. LUCA.
COG3409. LUCA.
COG5632. LUCA.
HOGENOMiHOG000273688.
InParanoidiP39800.
KOiK01447.
OMAiIYGPATK.
PhylomeDBiP39800.

Family and domain databases

CDDicd00118. LysM. 1 hit.
cd06583. PGRP. 1 hit.
Gene3Di1.10.101.10. 1 hit.
3.10.350.10. 1 hit.
3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR018392. LysM_dom.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01476. LysM. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00257. LysM. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF54106. SSF54106. 1 hit.
SSF55846. SSF55846. 1 hit.
PROSITEiPS51782. LYSM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39800-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNIIQDFIP VGANNRPGYA MTPLYITVHN TANTAVGADA AAHARYLKNP
60 70 80 90 100
DTTTSWHFTV DDTEIYQHLP LNENGWHAGD GNGSGNRASI GIEICENADG
110 120 130 140 150
DFAKATANAQ WLIKTLMAEH NISLANVVPH KYWSGKECPR KLLDTWDSFK
160 170 180 190 200
AGIGGGGSQT YVVKQGDTLT SIARAFGVTV AQLQEWNNIE DPNLIRVGQV
210 220 230 240 250
LIVSAPSAAE KPELYPLPDG IIQLTTPYTS GEHVFQVQRA LAALYFYPDK
260 270 280 290
GAVNNGIDGV YGPKTADAVA RFQSVNGLTA DGIYGPATKE KIAAQLS
Length:297
Mass (Da):31,913
Last modified:February 1, 1995 - v1
Checksum:i33DB710059A3EC72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36941 Genomic DNA. Translation: CAA85403.1.
L25924 Genomic DNA. Translation: AAA22645.1.
Z70177 Genomic DNA. Translation: CAA94049.1.
AL009126 Genomic DNA. Translation: CAB13138.1.
AJ002571 Genomic DNA. Translation: CAA05561.1.
PIRiI39938.
RefSeqiNP_389164.1. NC_000964.3.
WP_003245230.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13138; CAB13138; BSU12810.
GeneIDi939869.
KEGGibsu:BSU12810.
PATRICi18974313. VBIBacSub10457_1349.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36941 Genomic DNA. Translation: CAA85403.1.
L25924 Genomic DNA. Translation: AAA22645.1.
Z70177 Genomic DNA. Translation: CAA94049.1.
AL009126 Genomic DNA. Translation: CAB13138.1.
AJ002571 Genomic DNA. Translation: CAA05561.1.
PIRiI39938.
RefSeqiNP_389164.1. NC_000964.3.
WP_003245230.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HMBX-ray2.70A/B/C1-154[»]
3RDRX-ray2.20A1-154[»]
ProteinModelPortaliP39800.
SMRiP39800.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007101.

Proteomic databases

PaxDbiP39800.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13138; CAB13138; BSU12810.
GeneIDi939869.
KEGGibsu:BSU12810.
PATRICi18974313. VBIBacSub10457_1349.

Phylogenomic databases

eggNOGiENOG4108VPC. Bacteria.
COG1388. LUCA.
COG3409. LUCA.
COG5632. LUCA.
HOGENOMiHOG000273688.
InParanoidiP39800.
KOiK01447.
OMAiIYGPATK.
PhylomeDBiP39800.

Enzyme and pathway databases

BioCyciBSUB:BSU12810-MONOMER.

Family and domain databases

CDDicd00118. LysM. 1 hit.
cd06583. PGRP. 1 hit.
Gene3Di1.10.101.10. 1 hit.
3.10.350.10. 1 hit.
3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR018392. LysM_dom.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01476. LysM. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00257. LysM. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF54106. SSF54106. 1 hit.
SSF55846. SSF55846. 1 hit.
PROSITEiPS51782. LYSM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXLYA_BACSU
AccessioniPrimary (citable) accession number: P39800
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.