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UniProtKB/Swiss-Prot entry P71013


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

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Entry information
Entry name LEPT_BACSU
Primary accession number P71013
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on February 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 64)
Name and origin of the protein
Protein name Signal peptidase I T
Synonyms SPase I
EC 3.4.21.89
Leader peptidase I
Gene name
Name: sipT
OrderedLocusNames: BSU14410
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;
Tjalsma H., Bolhuis A., Bron S., Venema G., van Dijl J.M.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8969500 [NCBI, ExPASy, EBI, Israel, Japan]
Winters P., Caldwell R.M., Enfield L., Ferrari E.;
"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.";
Microbiology 142:3033-3037(1996).
[3]
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).
[4]
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).
[5]
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
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
U45883; AAB07348.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF012285; AAC24916.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99111; CAB13314.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G69707; G69707.
RefSeq NP_389324.1; -.
3D structure databases
HSSP P00803; 1B12. [HSSP ENTRY / PDB]
ModBase P71013.
Protein family/group databases
MEROPS S26.004; -.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1443-MON; -.
Organism-specific databases
SubtiList BG11977; sipT. [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.
ProtoNet P71013.
Genome annotation databases
GeneID 938763; -.
GenomeReviews AL009126_GR; BSU14410.
KEGG bsu:BSU14410; -.
NMPDR fig|224308.1.peg.1443; -.
Phylogenomic databases
HOGENOM P71013; -.
Genome annotation databases
CMR P71013; BSU14410.
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   193  193     Signal peptidase I T. PRO_0000109500
TOPO_DOM   1    25  25     Cytoplasmic (Potential). 
TRANSMEM   26    42  17     Potential. 
TOPO_DOM   43   193  151     Extracellular (Potential). 
ACT_SITE   51    51        By similarity. 
ACT_SITE   93    93        By similarity. 
Sequence information
Length: 193 AA [This is the length of the unprocessed precursor] Molecular weight: 21854 Da [This is the MW of the unprocessed precursor] CRC64: 6746B4C38037F3C9 [This is a checksum on the sequence]
        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 

P71013 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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NPSA logo NPSA Sequence analysis tools

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