ID   LEPT_BACSU              Reviewed;         193 AA.
AC   P71013;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 160.
DE   RecName: Full=Signal peptidase I T;
DE            Short=SPase I;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase I;
GN   Name=sipT; OrderedLocusNames=BSU14410;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Tjalsma H., Bolhuis A., Bron S., Venema G., van Dijl J.M.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969500; DOI=10.1099/13500872-142-11-3033;
RA   Winters P., Caldwell R.M., Enfield L., Ferrari E.;
RT   "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis
RT   168 chromosome: sequencing of a 27 kb segment and identification of several
RT   genes in the area.";
RL   Microbiology 142:3033-3037(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=9694797; DOI=10.1101/gad.12.15.2318;
RA   Tjalsma H., Bolhuis A., van Roosmalen M.L., Wiegert T., Schumann W.,
RA   Broekhuizen C.P., Quax W.J., Venema G., Bron S., van Dijl J.M.;
RT   "Functional analysis of the secretory precursor processing machinery of
RT   Bacillus subtilis: identification of a eubacterial homolog of archaeal and
RT   eukaryotic signal peptidases.";
RL   Genes Dev. 12:2318-2331(1998).
RN   [5]
RP   REVIEW.
RX   PubMed=9823656; DOI=10.1016/s0168-1656(98)00099-6;
RA   Bron S., Bolhuis A., Tjalsma H., Holsappel S., Venema G., van Dijl J.M.;
RT   "Protein secretion and possible roles for multiple signal peptidases for
RT   precursor processing in bacilli.";
RL   J. Biotechnol. 64:3-13(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC         from secreted and periplasmic proteins.; EC=3.4.21.89;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Expressed at the postexponential growth phase; regulated by
CC       the DegS-DegU system.
CC   -!- MISCELLANEOUS: B.subtilis contains five chromosomal type I signal
CC       peptidases: SipS, SipT, SipU, SipV and SipW. They have different, but
CC       overlapping, substrate specificities and have different transcription
CC       patterns.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
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DR   EMBL; U45883; AAB07348.1; -; Genomic_DNA.
DR   EMBL; AF012285; AAC24916.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13314.1; -; Genomic_DNA.
DR   PIR; G69707; G69707.
DR   RefSeq; NP_389324.1; NC_000964.3.
DR   RefSeq; WP_003232348.1; NC_000964.3.
DR   AlphaFoldDB; P71013; -.
DR   SMR; P71013; -.
DR   FunCoup; P71013; 515.
DR   STRING; 224308.BSU14410; -.
DR   MEROPS; S26.004; -.
DR   PaxDb; 224308-BSU14410; -.
DR   EnsemblBacteria; CAB13314; CAB13314; BSU_14410.
DR   GeneID; 86874053; -.
DR   GeneID; 938763; -.
DR   KEGG; bsu:BSU14410; -.
DR   PATRIC; fig|224308.179.peg.1571; -.
DR   eggNOG; COG0681; Bacteria.
DR   InParanoid; P71013; -.
DR   OrthoDB; 9802919at2; -.
DR   PhylomeDB; P71013; -.
DR   BioCyc; BSUB:BSU14410-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P71013; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0009003; F:signal peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   FunFam; 2.10.109.10:FF:000008; Signal peptidase I; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR   PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..193
FT                   /note="Signal peptidase I T"
FT                   /id="PRO_0000109500"
FT   TOPO_DOM        1..25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..193
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   193 AA;  21854 MW;  6746B4C38037F3C9 CRC64;
     MTEEKNTNTE KTAKKKTNTY LEWGKAIVIA VLLALLIRHF LFEPYLVEGS SMYPTLHDGE
     RLFVNKTVNY IGELKRGDIV IINGETSKIH YVKRLIGKPG ETVQMKDDTL YINGKKVAEP
     YLSKNKKEAE KLGVSLTGDF GPVKVPKGKY FVMGDNRLNS MDSRNGLGLI AEDRIVGTSK
     FVFFPFNEMR QTK
//