LEP_MYCLE
ID LEP_MYCLE Reviewed; 289 AA.
AC O33021;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Probable signal peptidase I;
DE Short=SPase I;
DE EC=3.4.21.89;
DE AltName: Full=Leader peptidase I;
GN Name=lepB; OrderedLocusNames=ML1612; ORFNames=MLCB250.39;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; Z97369; CAB10633.1; -; Genomic_DNA.
DR EMBL; AL583922; CAC30563.1; -; Genomic_DNA.
DR PIR; F87110; F87110.
DR RefSeq; NP_302111.1; NC_002677.1.
DR RefSeq; WP_010908432.1; NC_002677.1.
DR AlphaFoldDB; O33021; -.
DR SMR; O33021; -.
DR STRING; 272631.ML1612; -.
DR MEROPS; S26.024; -.
DR EnsemblBacteria; CAC30563; CAC30563; CAC30563.
DR KEGG; mle:ML1612; -.
DR PATRIC; fig|272631.5.peg.3038; -.
DR Leproma; ML1612; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_0_0_11; -.
DR OMA; HGCNGCV; -.
DR Proteomes; UP000000806; 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; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Probable signal peptidase I"
FT /id="PRO_0000109510"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 84
FT /evidence="ECO:0000250"
FT ACT_SITE 162
FT /evidence="ECO:0000250"
SQ SEQUENCE 289 AA; 31086 MW; 69F59B03944768DD CRC64;
MTETTDSVPE PPSDADQLQP KVSICGLDMP AEVSETAAEA AIGVSEPKKR SALWEFAILA
VIAIGLYYVM LTFVARPYLI PSESMEPTLH GCSGCVGDRI MVDKITYRFS SPQPGDVIVF
KGPPSWNTMY KSIRSNNIVL RSVQNALSFV GFVPPDENDL VKRVIAVGGQ TVQCRSDTGL
TVNGKPLKEP YLRPVTMNAD LSFSPCLGSE FGPVTVPQGR LWVMGDNRIH SADSRYHCNS
TDVVNGLSCT GDPNSGTVPV SNVIGKARVV VWPPSRWGGV GSVNSQQGQ