P71013 (LEPT_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Signal peptidase I T
Short name=SPase I
EC=3.4.21.89

Alternative name(s):
Leader peptidase I

Gene names

Name:	sipT
Ordered Locus Names:	BSU14410

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	193 AA.
Sequence status	Complete.
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; Single-pass type II membrane protein Potential.
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 Transmembrane helix
Molecular function	Hydrolase Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 193	193	Signal peptidase I T		PRO_0000109500
Regions
	Topological domain	1 – 25	25	Cytoplasmic Potential
	Transmembrane	26 – 42	17	Helical; Potential
	Topological domain	43 – 193	151	Extracellular Potential
Sites
	Active site	51	1	By similarity
	Active site	93	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P71013 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 6746B4C38037F3C9	FASTA	193	21,854
	10 20 30 40 50 60 MTEEKNTNTE KTAKKKTNTY LEWGKAIVIA VLLALLIRHF LFEPYLVEGS SMYPTLHDGE 70 80 90 100 110 120 RLFVNKTVNY IGELKRGDIV IINGETSKIH YVKRLIGKPG ETVQMKDDTL YINGKKVAEP 130 140 150 160 170 180 YLSKNKKEAE KLGVSLTGDF GPVKVPKGKY FVMGDNRLNS MDSRNGLGLI AEDRIVGTSK 190 FVFFPFNEMR QTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Tjalsma H., Bolhuis A., Bron S., Venema G., van Dijl J.M. Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis 168 chromosome: sequencing of a 27 kb segment and identification of several genes in the area." Winters P., Caldwell R.M., Enfield L., Ferrari E. Microbiology 142:3033-3037(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. , 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]	"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] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[5]	"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] [Europe PMC] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U45883 Genomic DNA. Translation: AAB07348.1. AF012285 Genomic DNA. Translation: AAC24916.1. AL009126 Genomic DNA. Translation: CAB13314.1.
PIR	G69707.
RefSeq	NP_389324.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P71013.
SMR	P71013. Positions 38-192.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU14410.
Protein family/group databases
MEROPS	S26.004.
Proteomic databases
PaxDb	P71013.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB13314; CAB13314; BSU14410.
GeneID	938763.
KEGG	bsu:BSU14410.
PATRIC	18974671. VBIBacSub10457_1527.
Organism-specific databases
GenoList	BSU14410. [Micado]
Phylogenomic databases
eggNOG	COG0681.
HOGENOM	HOG000003673.
KO	K03100.
OMA	EYAYNDD.
ProtClustDB	CLSK862274.
Enzyme and pathway databases
BioCyc	BSUB:BSU14410-MONOMER.
Family and domain databases
Gene3D	2.10.109.10. 2 hits.
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. IPR015927. Peptidase_S24_S26A/B/C. IPR011056. Peptidase_S24_S26A/B/C_b-rbn. [Graphical view]
PANTHER	PTHR12383. PTHR12383. 1 hit.
Pfam	PF00717. Peptidase_S24. 1 hit. [Graphical view]
PRINTS	PR00727. LEADERPTASE.
SUPFAM	SSF51306. Pept_S24_S26_C. 1 hit.
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

LEPT_BACSU

Accession

Primary (citable) accession number: P71013

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program