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Protein

N-acetylmuramoyl-L-alanine amidase BlyA

Gene

blyA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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

GO - Biological processi

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 Componenti: Chromosome

Organism-specific databases

GenoListiBSU21410. [Micado]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367N-acetylmuramoyl-L-alanine amidase BlyAPRO_0000164416Add
BLAST

Proteomic databases

PaxDbiO31982.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100011791.

Structurei

3D structure databases

ProteinModelPortaliO31982.
SMRiO31982. Positions 1-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5632.
HOGENOMiHOG000095240.
KOiK01447.
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

        10         20         30         40         50
MSVFTNSYIP VNKYTRPGLK LQGVKKCVLH YTANPGAGAD NHRRYFSNAQ
60 70 80 90 100
VYASAHIFVD KAEAICIIPL NEVAYHANDI QQRDSAGNPY RGVAALKPNA
110 120 130 140 150
NFLSIGVEMC LEKDGSFHSD TVERTEDVFV ELCNKFGLDP IDDIVRHYDI
160 170 180 190 200
THKNCPAPWV SNSQKFVDFK NRVKAKMSGK SVSKASPTKP TTSSPSSSSA
210 220 230 240 250
VSGSLKSKVD GLRFYSKPSW EDKDVVGTVN KGIGFPTVVE KVKVGSAYQY
260 270 280 290 300
KVKNSKGTTY YITASDKYVD VTGSVKTSSS APKTTSTSSS SSSIKSVGKI
310 320 330 340 350
KIVGVSSAAI VMDKPDRNSS KNIGTVKLGS TISISGSVKG KNNSNGYWEV
360
IYKGKRGYIS GQFGSTI
Length:367
Mass (Da):39,629
Last modified:January 1, 1998 - v1
Checksum:i20D8BA91DF6A982A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021803 Genomic DNA. Translation: AAC38300.1.
AL009126 Genomic DNA. Translation: CAB14059.1.
RefSeqiNP_390024.1. NC_000964.3.
WP_004399108.1. NZ_JNCM01000036.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021803 Genomic DNA. Translation: AAC38300.1.
AL009126 Genomic DNA. Translation: CAB14059.1.
RefSeqiNP_390024.1. NC_000964.3.
WP_004399108.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliO31982.
SMRiO31982. Positions 1-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100011791.

Proteomic databases

PaxDbiO31982.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU21410. [Micado]

Phylogenomic databases

eggNOGiCOG5632.
HOGENOMiHOG000095240.
KOiK01447.
OrthoDBiEOG6GR386.

Enzyme and pathway databases

BioCyciBSUB:BSU21410-MONOMER.

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.
ProtoNetiSearch...

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: June 24, 2015
This is version 85 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

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.