LEPT_BACSU
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 03-AUG-2022, entry version 144.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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; NZ_JNCM01000035.1.
DR AlphaFoldDB; P71013; -.
DR SMR; P71013; -.
DR STRING; 224308.BSU14410; -.
DR MEROPS; S26.004; -.
DR PaxDb; P71013; -.
DR EnsemblBacteria; CAB13314; CAB13314; BSU_14410.
DR GeneID; 938763; -.
DR KEGG; bsu:BSU14410; -.
DR PATRIC; fig|224308.179.peg.1571; -.
DR eggNOG; COG0681; Bacteria.
DR InParanoid; P71013; -.
DR OMA; ACDAYIK; -.
DR PhylomeDB; P71013; -.
DR BioCyc; BSUB:BSU14410-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR CDD; cd06530; S26_SPase_I; 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 PANTHER; PTHR43390; PTHR43390; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR02227; sigpep_I_bact; 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
