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P50864 (CWLD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. 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:
Germination-specific N-acetylmuramoyl-L-alanine amidase

EC=3.5.1.28
Alternative name(s):
Autolysin
Cell wall hydrolase
Gene names
Name:cwlD
Ordered Locus Names:BSU01530
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex. Ref.4

Catalytic activity

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Ref.4

Subcellular location

Secreted Potential.

Developmental stage

Expression of cwlD takes place in both the mother cell and forespore compartments of sporulating cells. Ref.4

Miscellaneous

CwlD and PdaA are necessary and sufficient for muramic delta-lactam production in B.subtilis spore peptidoglycan (Ref.4).

Sequence similarities

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

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 237210Germination-specific N-acetylmuramoyl-L-alanine amidase
PRO_0000164419

Sequences

Sequence LengthMass (Da)Tools
P50864 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E5B92E58552B59D6

FASTA23727,006
        10         20         30         40         50         60 
MRKKLKWLSF LLGFIILLFL FKYQFSNNDS WKPWSLPLSG KIIYLDPGHG GPDGGAVGGK 

        70         80         90        100        110        120 
LLEKDVTLEV AFRVRDYLQE QGALVIMTRE SDTDLAPEGT KGYSRRKAED LRQRVKLINH 

       130        140        150        160        170        180 
SEAELYISIH LNAIPSQKWS GAQSFYYGKY AENEKVAKYI QDELRRNLEN TTRKAKRIHG 

       190        200        210        220        230 
IYLMQNVTKP GALIEVGFLS NPSEATLLGK PKYQDKVASS IYKGILRYFT EKGDPPE 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and regulation of a new putative cell wall hydrolase gene, cwlD, which affects germination in Bacillus subtilis."
Sekiguchi J., Akeo K., Yamamoto H., Khasanov F.K., Alonso J.C., Kuroda A.
J. Bacteriol. 177:5582-5589(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus subtilis chromosome."
Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K., Kawamura F., Yoshikawa H., Takahashi H.
Microbiology 142:3039-3046(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"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.
[4]"Production of muramic delta-lactam in Bacillus subtilis spore peptidoglycan."
Gilmore M.E., Bandyopadhyay D., Dean A.M., Linnstaedt S.D., Popham D.L.
J. Bacteriol. 186:80-89(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74737 Genomic DNA. Translation: CAA52758.1.
D64126 Genomic DNA. Translation: BAA10993.1.
AL009126 Genomic DNA. Translation: CAB11929.1.
PIRG69610.
RefSeqNP_388034.1. NC_000964.3.

3D structure databases

ProteinModelPortalP50864.
SMRP50864. Positions 41-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU01530.

Proteomic databases

PaxDbP50864.

Protocols and materials databases

DNASU938917.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB11929; CAB11929; BSU01530.
GeneID938917.
KEGGbsu:BSU01530.
PATRIC18971817. VBIBacSub10457_0157.

Organism-specific databases

GenoListBSU01530. [Micado]

Phylogenomic databases

eggNOGCOG0860.
HOGENOMHOG000163501.
KOK01448.
OMAELYISIH.
OrthoDBEOG6CP3X3.
PhylomeDBP50864.

Enzyme and pathway databases

BioCycBSUB:BSU01530-MONOMER.

Family and domain databases

Gene3D3.40.630.40. 1 hit.
InterProIPR002508. CW_Hdrlase/autolysin_cat.
IPR014234. Spore_CwlD.
[Graphical view]
PfamPF01520. Amidase_3. 1 hit.
[Graphical view]
SMARTSM00646. Ami_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR02883. spore_cwlD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCWLD_BACSU
AccessionPrimary (citable) accession number: P50864
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 91 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