Reviewed, UniProtKB/Swiss-Prot P54450 (CWLH_BACSU)

Names and origin

Protein names

Recommended name:
    N-acetylmuramoyl-L-alanine amidase cwlH
    EC=3.5.1.28
Alternative name(s):
    Cell wall hydrolase
    Autolysin

Gene names

Name:	cwlH
Synonyms:	yqeE
Ordered Locus Names:	BSU25710

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Subcellular location	Secreted Potential.
Developmental stage	Expressed during the late sporulation phase.
Induction	Expression is gerE and sigma K-dependent.
Sequence similarities	Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.0.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Competence Sporulation
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW establishment of competence for transformation Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 44	44	Potential
	Chain	45 – 250	206	N-acetylmuramoyl-L-alanine amidase cwlH		PRO_0000006454

Sequences

	Sequence		Length	Mass (Da)
	P54450-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: E88E0AAD66533FC2	FASTA	250	27,571
	10 20 30 40 50 60 MVTIKKDFIP VSNDNRPGYA MAPAYITVHN TANTAKGADA KMHAKFVKNP NTSESWHFTV 70 80 90 100 110 120 DDSVIYQHLP IDENGWHAGD GTNGTGNRKS IGIEICENAD GDFEKATSNA QWLIRKLMKE 130 140 150 160 170 180 NNIPLNRVVP HKKWSGKECP RKLLDHWNSF LNGISSSDTP PKETSPSYPL PSGVIKLTSP 190 200 210 220 230 240 YRKGTNILQL QKALAVLHFY PDKGAKNNGI DGVYGPKTAN AVKRFQLMNG LTADGIYGPK 250 TKAKLKSKLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1996) [PubMed: 8969508] [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(1997) [PubMed: 9384377] [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(1999) [PubMed: 10515909] [Abstract] Cited for: CHARACTERIZATION. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D84432 Genomic DNA. Translation: BAA12441.1. AL009126 Genomic DNA. Translation: CAB14512.1.
PIR	A69951.
RefSeq	NP_390448.1.
3D structure databases
HSSP	HSSP built from PDB template 1LBU based on UniProtKB P00733.
ModBase	Search...
Genome annotation databases
GeneID	937808.
GenomeReviews	Gene locus BSU25710 in contig AL009126_GR.
KEGG	bsu:BSU25710.
NMPDR	fig|224308.1.peg.2573.
Organism-specific databases
SubtiList	BG11633. cwlH. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P54450.
OMA	RESISVE.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU2566-MON.
BRENDA	3.5.1.28. 150.
Family and domain databases
InterPro	IPR002502. Amidase_2. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Gene3D	G3DSA:3.40.80.10. Amidase_2. 1 hit. G3DSA:1.10.101.10. PGBD_1. 1 hit.
Pfam	PF01510. Amidase_2. 1 hit. PF01471. PG_binding_1. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CWLH_BACSU

Accession

Primary (citable) accession number: P54450

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)