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O32041 (YRVJ_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative N-acetylmuramoyl-L-alanine amidase YrvJ

EC=3.5.1.28
Gene names
Name:yrvJ
Ordered Locus Names:BSU27580
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Probably involved in cell-wall metabolism By similarity.

Catalytic activity

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

Subcellular location

Secretedcell wall By similarity.

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell wall
Secreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 518491Putative N-acetylmuramoyl-L-alanine amidase YrvJ
PRO_0000360805

Sequences

Sequence LengthMass (Da)Tools
O32041 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 8FE642A3D7724135

FASTA51855,501
        10         20         30         40         50         60 
MNKKYFVLIV CIIFTSALFP TFSSVTAAQG EAVIATDEMN VRSGPGLSYG ITAEVKKGER 

        70         80         90        100        110        120 
YPILKEDGDW VQIQLGSGEK GWVVSWLITK EDQASTSSSG SSDTVTSTDP DLRMRSGPGT 

       130        140        150        160        170        180 
SYEVIGKFPQ GSQASVIDKD SGWIKISYHS ATGWVSSEYV TSGGSSSASD ESDQTEDSGA 

       190        200        210        220        230        240 
STTGTVGVSS LNVRASASHD AAIITKLDRG TKLTVLNEKN GWAHIEVNGL KGWVASHYLL 

       250        260        270        280        290        300 
TSSVPADDSA NAGSSSSAKK AYIMYGGTNL RSDASTSASI VERAAKGDSY TITGSKGSWY 

       310        320        330        340        350        360 
EIKLDNGQTA YVANWVVQTS KSAEEAGEPP VSDSPSGNGS LNNKTIIVDP GHGGKDSGTI 

       370        380        390        400        410        420 
GYSGKFEKNL TIKTAKLLAS KLRSAGADVY VTRQDDTFVS LQSRVSTSHY RNADAFISIH 

       430        440        450        460        470        480 
YDSYADTSTR GSTAYYYSPA KDQELASDVH SEVVKRSSIP DRGVLFGDYY VLRENRQPAM 

       490        500        510 
LYELGYVSHP QEEAIVHSNS YQEKVTDGIE SGLEKYFQ 

« Hide

References

[1]"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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB14717.1.
PIRB69981.
RefSeqNP_390636.1. NC_000964.3.

3D structure databases

ProteinModelPortalO32041.
SMRO32041. Positions 29-166, 181-320, 344-518.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU27580.

Proteomic databases

PaxDbO32041.

Protocols and materials databases

DNASU937544.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14717; CAB14717; BSU27580.
GeneID937544.
KEGGbsu:BSU27580.
PATRIC18977380. VBIBacSub10457_2879.

Organism-specific databases

GenoListBSU27580.

Phylogenomic databases

eggNOGCOG0860.
HOGENOMHOG000018078.
KOK01448.
OMATSHYRNA.
OrthoDBEOG6CP3X3.
ProtClustDBCLSK887673.

Enzyme and pathway databases

BioCycBSUB:BSU27580-MONOMER.

Family and domain databases

Gene3D3.40.630.40. 1 hit.
InterProIPR002508. CW_Hdrlase/autolysin_cat.
IPR017293. N-acetylmuramoyl-L-ala_amidase.
IPR003646. SH3-like_bac-type.
[Graphical view]
PfamPF01520. Amidase_3. 1 hit.
PF08239. SH3_3. 4 hits.
[Graphical view]
PIRSFPIRSF037846. Autolysin_YrvJ_prd. 1 hit.
SMARTSM00646. Ami_3. 1 hit.
SM00287. SH3b. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameYRVJ_BACSU
AccessionPrimary (citable) accession number: O32041
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: November 13, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList