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UniProtKB/Swiss-Prot entry P28628


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LEPS_BACSU
Primary accession number P28628
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 76)
Name and origin of the protein
Protein name Signal peptidase I S
Synonyms SPase I
EC 3.4.21.89
Leader peptidase I
Gene name
Name: sipS
OrderedLocusNames: BSU23310
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / 6GM(AMY);
PubMed=1639057 [NCBI, ExPASy, EBI, Israel, Japan]
van Dijl J.M., de Jong A., Vehmaanpera J., Venema G., Bron S.;
"Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases.";
EMBO J. 11:2819-2828(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / Marburg;
PubMed=7934829 [NCBI, ExPASy, EBI, Israel, Japan]
Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
"The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data.";
Mol. Microbiol. 10:385-395(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
DOI=10.1074/jbc.270.8.3611; PubMed=7876097 [NCBI, ExPASy, EBI, Israel, Japan]
van Dijl J.M., de Jong A., Venema G., Bron S.;
"Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis. Structural and functional similarities with LexA-like proteases.";
J. Biol. Chem. 270:3611-3618(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[5]
CHARACTERIZATION.
PubMed=8951809 [NCBI, ExPASy, EBI, Israel, Japan]
Bolhuis A., Sorokin A., Azevedo V., Ehrlich S.D., Braun P.G., de Jong A., Venema G., Bron S., van Dijl J.M.;
"Bacillus subtilis can modulate its capacity and specificity for protein secretion through temporally controlled expression of the sipS gene for signal peptidase I.";
Mol. Microbiol. 22:605-618(1996).
[6]
CHARACTERIZATION.
PubMed=9694797 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases.";
Genes Dev. 12:2318-2331(1998).
[7]
FUNCTION OF TRANSMEMBRANE DOMAIN.
DOI=10.1074/jbc.M007093200; PubMed=10982814 [NCBI, ExPASy, EBI, Israel, Japan]
Carlos J.L., Paetzel M., Brubaker G., Karla A., Ashwell C.M., Lively M.O., Cao G., Bullinger P., Dalbey R.E.;
"The role of the membrane-spanning domain of type I signal peptidases in substrate cleavage site selection.";
J. Biol. Chem. 275:38813-38822(2000).
[8]
REVIEW.
DOI=10.1016/S0168-1656(98)00099-6; PubMed=9823656 [NCBI, ExPASy, EBI, Israel, Japan]
Bron S., Bolhuis A., Tjalsma H., Holsappel S., Venema G., van Dijl J.M.;
"Protein secretion and possible roles for multiple signal peptidases for precursor processing in bacilli.";
J. Biotechnol. 64:3-13(1998).
Comments
  • FUNCTION: Not essential for cell viability, but required for efficient secretion of many proteins.
  • 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.
  • SIMILARITY: Belongs to the peptidase S26 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z11847; CAA77871.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L09228; AAA67478.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99116; CAB14263.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S23381; S23381.
RefSeq NP_390212.1; -.
3D structure databases
HSSP P00803; 1B12. [HSSP ENTRY / PDB]
ModBase P28628.
Protein family/group databases
MEROPS S26.003; -.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2330-MON; -.
Organism-specific databases
SubtiList BG10515; sipS. [Micado]
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008236; Molecular function: serine-type peptidase activity (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000223; Pept_S26A_signal_pept_1.
IPR011056; Peptidase_S24_S26_C.
IPR014037; Peptidase_S26A.
Graphical view of domain structure.
Gene3D G3DSA:2.10.109.10; Pept_S24_S26_C; 1.
PANTHER PTHR12383:SF1; Pept_S26A_signal_pept_1; 1.
PTHR12383; Peptidase_S26A; 1.
Pfam PF00717; Peptidase_S24; 1.
Pfam graphical view of domain structure.
PRINTS PR00727; LEADERPTASE.
TIGRFAMs TIGR02227; sigpep_I_bact; 1.
PROSITE PS00501; SPASE_I_1; 1.
PS00760; SPASE_I_2; 1.
PS00761; SPASE_I_3; 1.
BLOCKS P28628.
ProtoNet P28628.
Genome annotation databases
GeneID 938944; -.
GenomeReviews AL009126_GR; BSU23310.
KEGG bsu:BSU23310; -.
NMPDR fig|224308.1.peg.2335; -.
Phylogenomic databases
HOGENOM P28628; -.
Genome annotation databases
CMR P28628; BSU23310.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Complete proteome; Hydrolase; Membrane; Protease; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   184  184     Signal peptidase I S. PRO_0000109499
TOPO_DOM   1    18  18     Cytoplasmic (Potential). 
TRANSMEM   19    39  21     Potential. 
TOPO_DOM   40   184  145     Extracellular (Potential). 
ACT_SITE   43    43         
ACT_SITE   83    83         
MUTAGEN   42    42        D->S: No effect. 
MUTAGEN   43    43        S->A,V: Loss of activity. 
MUTAGEN   43    43        S->C,T: Reduced activity. 
MUTAGEN   44    44        M->A: Increased activity. 
MUTAGEN   46    46        P->A: Slightly reduced activity. 
MUTAGEN   47    47        T->A: No effect. 
MUTAGEN   48    48        L->A: Reduced activity. 
MUTAGEN   69    69        G->A: Slightly reduced activity. 
MUTAGEN   70    70        D->A: Slightly reduced activity. 
MUTAGEN   71    71        I->A: Slightly reduced activity. 
MUTAGEN   72    72        V->A: No effect. 
MUTAGEN   74    74        L->A: Reduced activity. 
MUTAGEN   79    79        V->A: No effect. 
MUTAGEN   81    81        Y->A: Reduced activity. 
MUTAGEN   81    81        Y->F: No effect. 
MUTAGEN   83    83        K->A,H,R: Loss of activity. 
MUTAGEN   84    84        R->A: Loss of activity. 
MUTAGEN   84    84        R->H: Strongly reduced activity. 
MUTAGEN   84    84        R->K: No effect. 
MUTAGEN   86    86        I->A: Slightly reduced activity. 
MUTAGEN   87    87        G->A: No effect. 
MUTAGEN   88    88        L->A: Reduced activity. 
MUTAGEN   89    89        P->A: No effect. 
MUTAGEN   90    90        G->A: No effect. 
MUTAGEN   91    91        D->A,E,N: No effect. 
MUTAGEN   141   141        Y->A: No effect. 
MUTAGEN   145   145        G->A: Strongly reduced activity. 
MUTAGEN   146   146        D->A,N: Strongly reduced activity. 
MUTAGEN   146   146        D->E: No effect. 
MUTAGEN   147   147        N->A: Reduced activity. 
MUTAGEN   150   150        N->A: No effect. 
MUTAGEN   151   151        S->A: Reduced activity. 
MUTAGEN   153   153        D->A: Strongly reduced activity. 
MUTAGEN   153   153        D->E,N: Loss of activity. 
MUTAGEN   154   154        S->A: Slightly reduced activity. 
MUTAGEN   155   155        R->A: Reduced activity. 
Sequence information
Length: 184 AA [This is the length of the unprocessed precursor] Molecular weight: 21047 Da [This is the MW of the unprocessed precursor] CRC64: 5A2D005BF0D33CE9 [This is a checksum on the sequence]
        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 

P28628 in FASTA format

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View entry in raw text format (no links)
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