ID   LEP_HAEIN               Reviewed;         349 AA.
AC   P44454;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 139.
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=HI_0015;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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 inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
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DR   EMBL; L42023; AAC21693.1; -; Genomic_DNA.
DR   PIR; H64042; H64042.
DR   RefSeq; NP_438188.1; NC_000907.1.
DR   RefSeq; WP_005693886.1; NC_000907.1.
DR   AlphaFoldDB; P44454; -.
DR   SMR; P44454; -.
DR   STRING; 71421.HI_0015; -.
DR   MEROPS; S26.001; -.
DR   EnsemblBacteria; AAC21693; AAC21693; HI_0015.
DR   KEGG; hin:HI_0015; -.
DR   PATRIC; fig|71421.8.peg.15; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_1_1_6; -.
DR   OMA; SDSRFWG; -.
DR   PhylomeDB; P44454; -.
DR   BioCyc; HINF71421:G1GJ1-15-MON; -.
DR   Proteomes; UP000000579; 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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Protease;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..349
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109507"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..349
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   349 AA;  39734 MW;  8BAF091DCDF92F60 CRC64;
     MSNLFFVILL AVGFGVWKVL DYFQLPNTFS ILLLILTALS GVLWCYHRFV VLPKRHRQVA
     RAEQRSGKTL SEEEKAKIEP ISEASEFLSS LFPVLAVVFL VRSFLFEPFQ IPSGSMESTL
     RVGDFLVVNK YAYGVKDPIF QNTIIAGEKP QRGDVIVFKA PQQALIRTGL GATRAAFAEN
     LALSSKDNMS GVDYIKRIVG KGGDRVIFDV EQKTLKVVYG KEGKPCEIDC ETKAFEYTQN
     PTNPAFPNEL ELTEKGDVTH NVLISEYRRY SDLEFFPQEG MQTAEWLVPE GQYFVMGDHR
     DHSDDSRFWG FVPEKNIVGK ATYIWMSLEK EANEWPTGFR FERFFTAIK