Reviewed, UniProtKB/Swiss-Prot P28628 (LEPS_BACSU)

Names and origin

Protein names

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

Gene names

Name:	sipS
Ordered Locus Names:	BSU23310

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Not essential for cell viability, but required for efficient secretion of many proteins. Ref.7
Catalytic activity	Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Subcellular location	Cell membrane; Single-pass type II membrane protein.
Induction	Expressed at the postexponential growth phase; regulated by the degS-degU system.
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 S26 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
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	serine-type peptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 184	184	Signal peptidase I S		PRO_0000109499
Regions
	Topological domain	1 – 18	18	Cytoplasmic Potential
	Transmembrane	19 – 39	21	Potential
	Topological domain	40 – 184	145	Extracellular Potential
Sites
	Active site	43	1
	Active site	83	1
Experimental info
	Mutagenesis	42	1	D → S: No effect.
	Mutagenesis	43	1	S → A or V: Loss of activity.
	Mutagenesis	43	1	S → C or T: Reduced activity.
	Mutagenesis	44	1	M → A: Increased activity.
	Mutagenesis	46	1	P → A: Slightly reduced activity.
	Mutagenesis	47	1	T → A: No effect.
	Mutagenesis	48	1	L → A: Reduced activity.
	Mutagenesis	69	1	G → A: Slightly reduced activity.
	Mutagenesis	70	1	D → A: Slightly reduced activity.
	Mutagenesis	71	1	I → A: Slightly reduced activity.
	Mutagenesis	72	1	V → A: No effect.
	Mutagenesis	74	1	L → A: Reduced activity.
	Mutagenesis	79	1	V → A: No effect.
	Mutagenesis	81	1	Y → A: Reduced activity.
	Mutagenesis	81	1	Y → F: No effect.
	Mutagenesis	83	1	K → A, H or R: Loss of activity.
	Mutagenesis	84	1	R → A: Loss of activity.
	Mutagenesis	84	1	R → H: Strongly reduced activity.
	Mutagenesis	84	1	R → K: No effect.
	Mutagenesis	86	1	I → A: Slightly reduced activity.
	Mutagenesis	87	1	G → A: No effect.
	Mutagenesis	88	1	L → A: Reduced activity.
	Mutagenesis	89	1	P → A: No effect.
	Mutagenesis	90	1	G → A: No effect.
	Mutagenesis	91	1	D → A, E or N: No effect.
	Mutagenesis	141	1	Y → A: No effect.
	Mutagenesis	145	1	G → A: Strongly reduced activity.
	Mutagenesis	146	1	D → A or N: Strongly reduced activity.
	Mutagenesis	146	1	D → E: No effect.
	Mutagenesis	147	1	N → A: Reduced activity.
	Mutagenesis	150	1	N → A: No effect.
	Mutagenesis	151	1	S → A: Reduced activity.
	Mutagenesis	153	1	D → A: Strongly reduced activity.
	Mutagenesis	153	1	D → E or N: Loss of activity.
	Mutagenesis	154	1	S → A: Slightly reduced activity.
	Mutagenesis	155	1	R → A: Reduced activity.

Sequences

	Sequence		Length	Mass (Da)
	P28628-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 5A2D005BF0D33CE9	FASTA	184	21,047
	10 20 30 40 50 60 MKSENVSKKK SILEWAKAIV IAVVLALLIR NFIFAPYVVD GDSMYPTLHN RERVFVNMTV 70 80 90 100 110 120 KYIGEFDRGD IVVLNGDDVH YVKRIIGLPG DTVEMKNDQL YINGKKVDEP YLAANKKRAK 130 140 150 160 170 180 QDGFDHLTDD FGPVKVPDNK YFVMGDNRRN SMDSRNGLGL FTKKQIAGTS KFVFYPFNEM RKTN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases." van Dijl J.M., de Jong A., Vehmaanpera J., Venema G., Bron S. EMBO J. 11:2819-2828(1992) [PubMed: 1639057] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / 6GM(AMY).
[2]	"The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data." Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P. Mol. Microbiol. 10:385-395(1993) [PubMed: 7934829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg.
[3]	"Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis. Structural and functional similarities with LexA-like proteases." van Dijl J.M., de Jong A., Venema G., Bron S. J. Biol. Chem. 270:3611-3618(1995) [PubMed: 7876097] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS.
[4]	"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.
[5]	"Bacillus subtilis can modulate its capacity and specificity for protein secretion through temporally controlled expression of the sipS gene for signal peptidase I." Bolhuis A., Sorokin A., Azevedo V., Ehrlich S.D., Braun P.G., de Jong A., Venema G., Bron S., van Dijl J.M. Mol. Microbiol. 22:605-618(1996) [PubMed: 8951809] [Abstract] Cited for: CHARACTERIZATION.
[6]	"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.
[7]	"The role of the membrane-spanning domain of type I signal peptidases in substrate cleavage site selection." Carlos J.L., Paetzel M., Brubaker G., Karla A., Ashwell C.M., Lively M.O., Cao G., Bullinger P., Dalbey R.E. J. Biol. Chem. 275:38813-38822(2000) [PubMed: 10982814] [Abstract] Cited for: FUNCTION OF TRANSMEMBRANE DOMAIN.
[8]	"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	Z11847 Genomic DNA. Translation: CAA77871.1. L09228 Genomic DNA. Translation: AAA67478.1. AL009126 Genomic DNA. Translation: CAB14263.1.
PIR	S23381.
RefSeq	NP_390212.1.
3D structure databases
HSSP	HSSP built from PDB template 1B12 based on UniProtKB P00803.
ModBase	Search...
Protein family/group databases
MEROPS	S26.003.
Genome annotation databases
GeneID	938944.
GenomeReviews	Gene locus BSU23310 in contig AL009126_GR.
KEGG	bsu:BSU23310.
NMPDR	fig|224308.1.peg.2335.
Organism-specific databases
SubtiList	BG10515. sipS. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P28628.
OMA	ATVENDK.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU2330-MON.
BRENDA	3.4.21.89. 150.
Family and domain databases
InterPro	IPR000223. Pept_S26A_signal_pept_1. IPR019758. Pept_S26A_signal_pept_1_CS. IPR019757. Pept_S26A_signal_pept_1_Lys-AS. IPR019756. Pept_S26A_signal_pept_1_Ser-AS. IPR019759. Peptidase_S24_S26_cons-reg. IPR011056. Peptidase_S24_S26A/B/C_b-rbn. [Graphical view]
Gene3D	G3DSA:2.10.109.10. Pept_S24_S26_C. 1 hit.
Pfam	PF00717. Peptidase_S24. 1 hit. [Graphical view]
PRINTS	PR00727. LEADERPTASE.
TIGRFAMs	TIGR02227. sigpep_I_bact. 1 hit.
PROSITE	PS00501. SPASE_I_1. 1 hit. PS00760. SPASE_I_2. 1 hit. PS00761. SPASE_I_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEPS_BACSU

Accession

Primary (citable) accession number: P28628

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	November 3, 2009
This is version 83 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)