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O31982

- BLYA_BACSU

UniProt

O31982 - BLYA_BACSU

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Protein
N-acetylmuramoyl-L-alanine amidase BlyA
Gene
blyA, yomC, BSU21410
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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. Involved in prophage SP-beta-mediated cell lysis.1 Publication

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. establishment of competence for transformation Source: UniProtKB-KW
  2. peptidoglycan catabolic process Source: InterPro
  3. 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:BSU21410-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylmuramoyl-L-alanine amidase BlyA (EC:3.5.1.28)
Alternative name(s):
Autolysin
Cell wall hydrolase
Gene namesi
Name:blyA
Synonyms:yomC
Ordered Locus Names:BSU21410
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU21410. [Micado]

Subcellular locationi

Secreted Reviewed prediction

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
Chaini1 – 367367N-acetylmuramoyl-L-alanine amidase BlyA
PRO_0000164416Add
BLAST

Proteomic databases

PaxDbiO31982.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU21410.

Structurei

3D structure databases

ProteinModelPortaliO31982.
SMRiO31982. Positions 1-173.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5632.
HOGENOMiHOG000095240.
KOiK01447.
OMAiEHTIPIN.
OrthoDBiEOG6GR386.

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.

Sequencei

Sequence statusi: Complete.

O31982-1 [UniParc]FASTAAdd to Basket

« Hide

MSVFTNSYIP VNKYTRPGLK LQGVKKCVLH YTANPGAGAD NHRRYFSNAQ    50
VYASAHIFVD KAEAICIIPL NEVAYHANDI QQRDSAGNPY RGVAALKPNA 100
NFLSIGVEMC LEKDGSFHSD TVERTEDVFV ELCNKFGLDP IDDIVRHYDI 150
THKNCPAPWV SNSQKFVDFK NRVKAKMSGK SVSKASPTKP TTSSPSSSSA 200
VSGSLKSKVD GLRFYSKPSW EDKDVVGTVN KGIGFPTVVE KVKVGSAYQY 250
KVKNSKGTTY YITASDKYVD VTGSVKTSSS APKTTSTSSS SSSIKSVGKI 300
KIVGVSSAAI VMDKPDRNSS KNIGTVKLGS TISISGSVKG KNNSNGYWEV 350
IYKGKRGYIS GQFGSTI 367
Length:367
Mass (Da):39,629
Last modified:January 1, 1998 - v1
Checksum:i20D8BA91DF6A982A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF021803 Genomic DNA. Translation: AAC38300.1.
AL009126 Genomic DNA. Translation: CAB14059.1.
RefSeqiNP_390024.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB14059; CAB14059; BSU21410.
GeneIDi939130.
KEGGibsu:BSU21410.
PATRICi18976087. VBIBacSub10457_2234.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF021803 Genomic DNA. Translation: AAC38300.1 .
AL009126 Genomic DNA. Translation: CAB14059.1 .
RefSeqi NP_390024.1. NC_000964.3.

3D structure databases

ProteinModelPortali O31982.
SMRi O31982. Positions 1-173.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU21410.

Proteomic databases

PaxDbi O31982.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14059 ; CAB14059 ; BSU21410 .
GeneIDi 939130.
KEGGi bsu:BSU21410.
PATRICi 18976087. VBIBacSub10457_2234.

Organism-specific databases

GenoListi BSU21410. [Micado ]

Phylogenomic databases

eggNOGi COG5632.
HOGENOMi HOG000095240.
KOi K01447.
OMAi EHTIPIN.
OrthoDBi EOG6GR386.

Enzyme and pathway databases

BioCyci BSUB:BSU21410-MONOMER.

Family and domain databases

Gene3Di 3.40.80.10. 1 hit.
InterProi IPR002502. Amidase_domain.
[Graphical view ]
Pfami PF01510. Amidase_2. 1 hit.
[Graphical view ]
SMARTi SM00644. Ami_2. 1 hit.
[Graphical view ]
SUPFAMi SSF55846. SSF55846. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The N-acetylmuramoyl-L-alanine amidase encoded by the Bacillus subtilis 168 prophage SP beta."
    Regamey A., Karamata D.
    Microbiology 144:885-893(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: 168.
  2. "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.

Entry informationi

Entry nameiBLYA_BACSU
AccessioniPrimary (citable) accession number: O31982
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 80 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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