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P28628 (LEPS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type peptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 184184Signal peptidase I S
PRO_0000109499

Regions

Topological domain1 – 1818Cytoplasmic Potential
Transmembrane19 – 3921Helical; Potential
Topological domain40 – 184145Extracellular Potential

Sites

Active site431
Active site831

Experimental info

Mutagenesis421D → S: No effect.
Mutagenesis431S → A or V: Loss of activity.
Mutagenesis431S → C or T: Reduced activity.
Mutagenesis441M → A: Increased activity.
Mutagenesis461P → A: Slightly reduced activity.
Mutagenesis471T → A: No effect.
Mutagenesis481L → A: Reduced activity.
Mutagenesis691G → A: Slightly reduced activity.
Mutagenesis701D → A: Slightly reduced activity.
Mutagenesis711I → A: Slightly reduced activity.
Mutagenesis721V → A: No effect.
Mutagenesis741L → A: Reduced activity.
Mutagenesis791V → A: No effect.
Mutagenesis811Y → A: Reduced activity.
Mutagenesis811Y → F: No effect.
Mutagenesis831K → A, H or R: Loss of activity.
Mutagenesis841R → A: Loss of activity.
Mutagenesis841R → H: Strongly reduced activity.
Mutagenesis841R → K: No effect.
Mutagenesis861I → A: Slightly reduced activity.
Mutagenesis871G → A: No effect.
Mutagenesis881L → A: Reduced activity.
Mutagenesis891P → A: No effect.
Mutagenesis901G → A: No effect.
Mutagenesis911D → A, E or N: No effect.
Mutagenesis1411Y → A: No effect.
Mutagenesis1451G → A: Strongly reduced activity.
Mutagenesis1461D → A or N: Strongly reduced activity.
Mutagenesis1461D → E: No effect.
Mutagenesis1471N → A: Reduced activity.
Mutagenesis1501N → A: No effect.
Mutagenesis1511S → A: Reduced activity.
Mutagenesis1531D → A: Strongly reduced activity.
Mutagenesis1531D → E or N: Loss of activity.
Mutagenesis1541S → A: Slightly reduced activity.
Mutagenesis1551R → A: Reduced activity.

Sequences

Sequence LengthMass (Da)Tools
P28628 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 5A2D005BF0D33CE9

FASTA18421,047
        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

« Hide

References

« Hide '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 / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[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. expand/collapse author list , 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

EMBL
GenBank
DDBJ		Z11847 Genomic DNA. Translation: CAA77871.1.
L09228 Genomic DNA. Translation: AAA67478.1.
AL009126 Genomic DNA. Translation: CAB14263.1.
PIRS23381.
RefSeqNP_390212.1. NC_000964.3.

3D structure databases

ProteinModelPortalP28628.
SMRP28628. Positions 35-86.
ModBaseSearch...

Protein family/group databases

MEROPSS26.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001132; EBBACP00000001132; EBBACG00000001130.
GeneID938944.
GenomeReviewsGene locus BSU23310 in contig AL009126_GR.
KEGGbsu:BSU23310.
NMPDRfig|224308.1.peg.2335.
PATRIC18976477. VBIBacSub10457_2429.

Organism-specific databases

GenoListBSU23310. [Micado]

Phylogenomic databases

GeneTreeEBGT00070000031959.
HOGENOMHBG596607.
OMAEDEVFIN.
PhylomeDBP28628.
ProtClustDBCLSK862274.

Enzyme and pathway databases

BioCycBSUB:BSU23310-MONOMER.
BRENDA3.4.21.89. 700.

Family and domain databases

InterProIPR000223. 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]
Gene3DG3DSA:2.10.109.10. Pept_S24_S26_C. 2 hits.
KOK03100.
PfamPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00727. LEADERPTASE.
SUPFAMSSF51306. Pept_S24_S26_C. 1 hit.
TIGRFAMsTIGR02227. Sigpep_I_bact. 1 hit.
PROSITEPS00501. SPASE_I_1. 1 hit.
PS00760. SPASE_I_2. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEPS_BACSU
AccessionPrimary (citable) accession number: P28628
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents