ID   PECA_MYCTO              Reviewed;         558 AA.
AC   P9WIF0; L0T8F8; Q10873;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=PE cleavage protein A {ECO:0000250|UniProtKB:B2HE92};
DE   AltName: Full=PE-PGRS family protein PE_PGRS35 {ECO:0000305};
GN   Name=pecA {ECO:0000250|UniProtKB:B2HE92}; Synonyms=PE_PGRS35;
GN   OrderedLocusNames=MT2036;
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   -!- FUNCTION: Aspartic protease that processes the lipase LipY and other
CC       PE_PGRS proteins. Can also cleave itself.
CC       {ECO:0000250|UniProtKB:B2HE92}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:B2HE92}. Cell
CC       surface {ECO:0000250|UniProtKB:B2HE92}. Note=Secreted via the ESX-5 /
CC       type VII secretion system (T7SS). {ECO:0000250|UniProtKB:B2HE92}.
CC   -!- PTM: Undergoes auto-proteolytic processing.
CC       {ECO:0000250|UniProtKB:B2HE92}.
CC   -!- SIMILARITY: Belongs to the mycobacterial PE family. PGRS subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK46311.1; -; Genomic_DNA.
DR   PIR; E70756; E70756.
DR   RefSeq; WP_003899118.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIF0; -.
DR   SMR; P9WIF0; -.
DR   EnsemblBacteria; AAK46311; AAK46311; MT2036.
DR   KEGG; mtc:MT2036; -.
DR   PATRIC; fig|83331.31.peg.2191; -.
DR   HOGENOM; CLU_038249_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; -; 1.
DR   InterPro; IPR000084; PE-PGRS_N.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   Pfam; PF00934; PE; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Hydrolase; Protease; Secreted.
FT   CHAIN           1..558
FT                   /note="PE cleavage protein A"
FT                   /id="PRO_0000428018"
FT   DOMAIN          1..93
FT                   /note="PE"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000250|UniProtKB:B2HE92"
SQ   SEQUENCE   558 AA;  53738 MW;  17ECBE43778E021E CRC64;
     MSFLVVVPEF LTSAAADVEN IGSTLRAANA AAAASTTALA AAGADEVSAA VAALFARFGQ
     EYQAVSAQAS AFHQQFVQTL NSASGSYAAA EATIASQLQT AQHDLLGAVN APTETLLGRP
     LIGDGAPGTA TSPNGGAGGL LYGNGGNGYS ATASGVGGGA GGSAGLIGNG GAGGAGGPNA
     PGGAGGNGGW LLGNGGIGGP GGASSIPGMS GGAGGTGGAA GLLGWGANGG AGGLGDGVGV
     DRGTGGAGGR GGLLYGGYGV SGPGGDGRTV PLEIIHVTEP TVHANVNGGP TSTILVDTGS
     AGLVVSPEDV GGILGVLHMG LPTGLSISGY SGGLYYIFAT YTTTVDFGNG IVTAPTAVNV
     VLLSIPTSPF AISTYFSALL ADPTTTPFEA YFGAVGVDGV LGVGPNAVGP GPSIPTMALP
     GDLNQGVLID APAGELVFGP NPLPAPNVEV VGSPITTLYV KIDGGTPIPV PSIIDSGGVT
     GTIPSYVIGS GTLPANTNIE VYTSPGGDRL YAFNTNDYRP TVISSGLMNT GFLPFRFQPV
     YIDYSPSGIG TTVFDHPA