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Protein

N-acetylmuramoyl-L-alanine amidase CwlH

Gene

cwlH

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. Could play a role in mother cell lysis with CwlC.

Catalytic activityi

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

pH dependencei

Optimum pH is 7.0.

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:BSU25710-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylmuramoyl-L-alanine amidase CwlH (EC:3.5.1.28)
Alternative name(s):
Autolysin
Cell wall hydrolase
Gene namesi
Name:cwlH
Synonyms:yqeE
Ordered Locus Names:BSU25710
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU25710. [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 – 250206N-acetylmuramoyl-L-alanine amidase CwlHPRO_0000006454Add
BLAST

Proteomic databases

PaxDbiP54450.

Expressioni

Developmental stagei

Expressed during the late sporulation phase.

Inductioni

Expression is GerE and sigma K-dependent.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU25710.

Structurei

3D structure databases

SMRiP54450. Positions 2-154, 171-249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3409.
HOGENOMiHOG000273688.
InParanoidiP54450.
KOiK01447.
OMAiDENGWHA.
OrthoDBiEOG67T5NN.
PhylomeDBiP54450.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF55846. SSF55846. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54450-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTIKKDFIP VSNDNRPGYA MAPAYITVHN TANTAKGADA KMHAKFVKNP
60 70 80 90 100
NTSESWHFTV DDSVIYQHLP IDENGWHAGD GTNGTGNRKS IGIEICENAD
110 120 130 140 150
GDFEKATSNA QWLIRKLMKE NNIPLNRVVP HKKWSGKECP RKLLDHWNSF
160 170 180 190 200
LNGISSSDTP PKETSPSYPL PSGVIKLTSP YRKGTNILQL QKALAVLHFY
210 220 230 240 250
PDKGAKNNGI DGVYGPKTAN AVKRFQLMNG LTADGIYGPK TKAKLKSKLK
Length:250
Mass (Da):27,571
Last modified:October 1, 1996 - v1
Checksum:iE88E0AAD66533FC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84432 Genomic DNA. Translation: BAA12441.1.
AL009126 Genomic DNA. Translation: CAB14512.1.
PIRiA69951.
RefSeqiNP_390448.1. NC_000964.3.
WP_003229963.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14512; CAB14512; BSU25710.
GeneIDi937808.
KEGGibsu:BSU25710.
PATRICi18976984. VBIBacSub10457_2681.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84432 Genomic DNA. Translation: BAA12441.1.
AL009126 Genomic DNA. Translation: CAB14512.1.
PIRiA69951.
RefSeqiNP_390448.1. NC_000964.3.
WP_003229963.1. NZ_JNCM01000036.1.

3D structure databases

SMRiP54450. Positions 2-154, 171-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU25710.

Proteomic databases

PaxDbiP54450.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14512; CAB14512; BSU25710.
GeneIDi937808.
KEGGibsu:BSU25710.
PATRICi18976984. VBIBacSub10457_2681.

Organism-specific databases

GenoListiBSU25710. [Micado]

Phylogenomic databases

eggNOGiCOG3409.
HOGENOMiHOG000273688.
InParanoidiP54450.
KOiK01447.
OMAiDENGWHA.
OrthoDBiEOG67T5NN.
PhylomeDBiP54450.

Enzyme and pathway databases

BioCyciBSUB:BSU25710-MONOMER.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF55846. SSF55846. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
    Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
    Microbiology 142:3103-3111(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / JH642.
  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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Characterization of a new sigma-K-dependent peptidoglycan hydrolase gene that plays a role in Bacillus subtilis mother cell lysis."
    Nugroho F.A., Yamamoto H., Kobayashi Y., Sekiguchi J.
    J. Bacteriol. 181:6230-6237(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: 168.

Entry informationi

Entry nameiCWLH_BACSU
AccessioniPrimary (citable) accession number: P54450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 1, 2015
This is version 103 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.