Reviewed, UniProtKB/Swiss-Prot P54506 (LEPW_BACSU)

Names and origin

Protein names

Recommended name:
    Signal peptidase I W
      Short name=SPase I
    EC=3.4.21.89
Alternative name(s):
    Leader peptidase I

Gene names

Name:	sipW
Synonyms:	yqhE
Ordered Locus Names:	BSU24630

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	190 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Subcellular location	Cell membrane; Multi-pass membrane protein Potential.
Induction	Expressed constitutively.
Miscellaneous	B.subtilis contains five chromosomal type I signal peptidases: sipS, sipT, sipU, sipV and sipW. They have different, but overlapping, substrate specificities and have different transcription patterns.
Sequence similarities	Belongs to the peptidase S26B family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	Hydrolase Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro signal peptide processing Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 190	190	Signal peptidase I W		PRO_0000109539
Regions
	Transmembrane	4 – 24	21	Potential
	Transmembrane	143 – 163	21	Potential
Sites
	Active site	45	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P54506-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 0F3FBD2F08D2BB3C	FASTA	190	20,678
	10 20 30 40 50 60 MKLISNILYV IIFTLIIVLT LVVISTRSSG GEPAVFGYTL KSVLSGSMEP EFNTGSLILV 70 80 90 100 110 120 KEITDVKELQ KGDVITFMQD ANTAVTHRIV DITKQGDHLL FKTKGDNNAA ADSAPVSDEN 130 140 150 160 170 180 VRAQYTGFQL PYAGYMLHFA SQPIGTAVLL IVPGVMLLVY AFVTISSAIR EIERKTKALE 190 TDTKDSTMST

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]	"Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases." Tjalsma H., Bolhuis A., van Roosmalen M.L., Wiegert T., Schumann W., Broekhuizen C.P., Quax W.J., Venema G., Bron S., van Dijl J.M. Genes Dev. 12:2318-2331(1998) [PubMed: 9694797] [Abstract] Cited for: CHARACTERIZATION.
[4]	"Protein secretion and possible roles for multiple signal peptidases for precursor processing in bacilli." Bron S., Bolhuis A., Tjalsma H., Holsappel S., Venema G., van Dijl J.M. J. Biotechnol. 64:3-13(1998) [PubMed: 9823656] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D84432 Genomic DNA. Translation: BAA12540.1. AL009126 Genomic DNA. Translation: CAB14394.1.
PIR	B69708.
RefSeq	NP_390343.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	S26.011.
Genome annotation databases
GeneID	938542.
GenomeReviews	Gene locus BSU24630 in contig AL009126_GR.
KEGG	bsu:BSU24630.
NMPDR	fig|224308.1.peg.2467.
Organism-specific databases
SubtiList	BG11696. sipW. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P54506.
OMA	P54506. VITHRIT.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU2461-MON.
BRENDA	3.4.21.89. 150.
Family and domain databases
InterPro	IPR019759. Peptidase_S24_S26_cons-reg. IPR001733. Peptidase_S26B. [Graphical view]
PANTHER	PTHR10806. Peptidase_S26B. 1 hit.
Pfam	PF00717. Peptidase_S24. 1 hit. [Graphical view]
PRINTS	PR00728. SIGNALPTASE.
TIGRFAMs	TIGR02228. sigpep_I_arch. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LEPW_BACSU

Accession

Primary (citable) accession number: P54506

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 65 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)