Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

  1. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. establishment of competence for transformation Source: UniProtKB-KW
  3. peptidoglycan catabolic process Source: InterPro
  4. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
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
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU12810. [Micado]

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4444Sequence AnalysisAdd
BLAST
Chaini45 – 297253N-acetylmuramoyl-L-alanine amidase XlyAPRO_0000006457Add
BLAST

Proteomic databases

PaxDbiP39800.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU12810.

Structurei

Secondary structure

1
297
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Beta strandi25 – 306Combined sources
Helixi40 – 478Combined sources
Beta strandi57 – 604Combined sources
Beta strandi65 – 673Combined sources
Beta strandi78 – 803Combined sources
Helixi84 – 874Combined sources
Beta strandi88 – 947Combined sources
Helixi102 – 11918Combined sources
Helixi124 – 1263Combined sources
Beta strandi127 – 1293Combined sources
Helixi130 – 1345Combined sources
Turni140 – 1423Combined sources
Helixi143 – 1453Combined sources
Helixi146 – 1516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HMBX-ray2.70A/B/C1-154[»]
3RDRX-ray2.20A1-154[»]
ProteinModelPortaliP39800.
SMRiP39800. Positions 2-154, 223-295.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati161 – 20444LysMAdd
BLAST

Sequence similaritiesi

Contains 1 LysM repeat.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3409.
HOGENOMiHOG000273688.
InParanoidiP39800.
KOiK01447.
OMAiWHAGDGN.
OrthoDBiEOG6XHC2R.
PhylomeDBiP39800.

Family and domain databases

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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3HMBX-ray2.70A/B/C1-154[»]
3RDRX-ray2.20A1-154[»]
ProteinModelPortaliP39800.
SMRiP39800. Positions 2-154, 223-295.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU12810.

Proteomic databases

PaxDbiP39800.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU12810. [Micado]

Phylogenomic databases

eggNOGiCOG3409.
HOGENOMiHOG000273688.
InParanoidiP39800.
KOiK01447.
OMAiWHAGDGN.
OrthoDBiEOG6XHC2R.
PhylomeDBiP39800.

Enzyme and pathway databases

BioCyciBSUB:BSU12810-MONOMER.

Family and domain databases

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Krogh S., Joergensen S.T., Diderichsen B., Devine K.M.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / SO113.
  2. "Lytic enzymes associated with defective prophages of Bacillus subtilis: sequencing and characterization of the region comprising the N-acetylmuramoyl-L-alanine amidase gene of prophage PBSX."
    Longchamp P.F., Mauel C., Karamata D.
    Microbiology 140:1855-1867(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "Lysis genes of the Bacillus subtilis defective prophage PBSX."
    Krogh S., Jorgensen S.T., Devine K.M.
    J. Bacteriol. 180:2110-2117(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  4. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  5. "Sequence of the Bacillus subtilis genome between xlyA and ykoR."
    Devine K.M.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-297.
    Strain: 168.

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: January 7, 2015
This is version 110 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

External Data

Dasty 3

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 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.