ID   LEP_MYCTO               Reviewed;         294 AA.
AC   P9WKA0; L0TAZ5; Q10789;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Signal peptidase I;
DE            Short=SPase I;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase I;
GN   Name=lepB; OrderedLocusNames=MT2971;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47297.1; -; Genomic_DNA.
DR   PIR; B70927; B70927.
DR   RefSeq; WP_003414715.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKA0; -.
DR   SMR; P9WKA0; -.
DR   MEROPS; S26.024; -.
DR   EnsemblBacteria; AAK47297; AAK47297; MT2971.
DR   GeneID; 45426890; -.
DR   KEGG; mtc:MT2971; -.
DR   PATRIC; fig|83331.31.peg.3211; -.
DR   HOGENOM; CLU_028723_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
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; 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; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..294
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000427690"
FT   TOPO_DOM        1..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..294
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        96
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   294 AA;  31880 MW;  BBCAE8ADF68F897D CRC64;
     MTETTDSPSE RQPGPAEPEL SSRDPDIAGQ VFDAAPFDAA PDADSEGDSK AAKTDEPRPA
     KRSTLREFAV LAVIAVVLYY VMLTFVARPY LIPSESMEPT LHGCSTCVGD RIMVDKLSYR
     FGSPQPGDVI VFRGPPSWNV GYKSIRSHNV AVRWVQNALS FIGFVPPDEN DLVKRVIAVG
     GQTVQCRSDT GLTVNGRPLK EPYLDPATMM ADPSIYPCLG SEFGPVTVPP GRVWVMGDNR
     THSADSRAHC PLLCTDDPLP GTVPVANVIG KARLIVWPPS RWGVVRSVNP QQGR