ID   PECA_MYCMM              Reviewed;         553 AA.
AC   B2HE92;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=PE cleavage protein A {ECO:0000303|PubMed:31662454};
DE   AltName: Full=PE-PGRS family protein;
GN   Name=pecA {ECO:0000303|PubMed:31662454};
GN   OrderedLocusNames=MMAR_2933 {ECO:0000312|EMBL:ACC41372.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19602152; DOI=10.1111/j.1365-2958.2009.06783.x;
RA   Abdallah A.M., Verboom T., Weerdenburg E.M., Gey van Pittius N.C.,
RA   Mahasha P.W., Jimenez C., Parra M., Cadieux N., Brennan M.J.,
RA   Appelmelk B.J., Bitter W.;
RT   "PPE and PE_PGRS proteins of Mycobacterium marinum are transported via the
RT   type VII secretion system ESX-5.";
RL   Mol. Microbiol. 73:329-340(2009).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, DISRUPTION PHENOTYPE,
RP   MUTAGENESIS OF ASP-293, AND ACTIVE SITE.
RX   PubMed=31662454; DOI=10.1128/mbio.01951-19;
RA   Burggraaf M.J., Speer A., Meijers A.S., Ummels R., van der Sar A.M.,
RA   Korotkov K.V., Bitter W., Kuijl C.;
RT   "Type VII secretion substrates of pathogenic Mycobacteria are processed by
RT   a surface protease.";
RL   MBio 10:E01951-E01951(2019).
CC   -!- FUNCTION: Aspartic protease that processes the lipase LipY and other
CC       PE_PGRS proteins. Can also cleave itself. Cleaves LipY both inside the
CC       PE domain, before amino acid 98, and after amino acids 136 and 149.
CC       Involved in virulence. {ECO:0000269|PubMed:31662454}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19602152}. Cell
CC       surface {ECO:0000269|PubMed:31662454}. Note=Secreted via the ESX-5 /
CC       type VII secretion system (T7SS). {ECO:0000269|PubMed:19602152}.
CC   -!- PTM: Undergoes auto-proteolytic processing.
CC       {ECO:0000269|PubMed:31662454}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene does not affect LipY
CC       surface localization. Mutant shows moderate attenuation in the
CC       zebrafish larva infection model. {ECO:0000269|PubMed:31662454}.
CC   -!- SIMILARITY: Belongs to the mycobacterial PE family. PGRS subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000854; ACC41372.1; -; Genomic_DNA.
DR   RefSeq; WP_012394630.1; NC_010612.1.
DR   AlphaFoldDB; B2HE92; -.
DR   SMR; B2HE92; -.
DR   STRING; 216594.MMAR_2933; -.
DR   EnsemblBacteria; ACC41372; ACC41372; MMAR_2933.
DR   KEGG; mmi:MMAR_2933; -.
DR   eggNOG; COG3391; Bacteria.
DR   HOGENOM; CLU_038249_0_0_11; -.
DR   OMA; TPFDAYF; -.
DR   OrthoDB; 1329172at2; -.
DR   Proteomes; UP000001190; 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   1: Evidence at protein level;
KW   Aspartyl protease; Hydrolase; Protease; Reference proteome; Secreted;
KW   Virulence.
FT   CHAIN           1..553
FT                   /note="PE cleavage protein A"
FT                   /id="PRO_0000449880"
FT   DOMAIN          1..92
FT                   /note="PE"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000305|PubMed:31662454"
FT   MUTAGEN         293
FT                   /note="D->G: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:31662454"
SQ   SEQUENCE   553 AA;  53298 MW;  93A5625346A0E10C CRC64;
     MSLLVVAPEW LTSAAAELQS IESALSAANA AAAVPTTGLA AAAADEVSTA VATLFAGFGQ
     EYQAISTQLS AFQQQFALTL NSSAGSYSAA EAQSVSILDT LGQDVFGAIN APTEALLGRP
     LIGNGANGTA TSPNGGAGGL LFGNGGIGYS QTGAGIVGGA GGSAGLIGNG GAGGTGGAGA
     TGGAGGNGGW LFGSGGIGGT GGANALGTGG TGGLGGSAGL FGGGGNGGAG GLGISGDLGT
     GGAGGTGGFL LGDYGVSGAG GDGRTVPLEV VNVTEPVVNV NVNGGHSTPV LIDTGSAGLV
     MQVKDVGGPL GLLRMGLPSG ISMSAYSGGL TYLFATYPTT VDFGNGIVTS TTGVDVVLFS
     IPTSPYALTT WLNALWSNPL TTPFDAYFQS AGVDGVLGVG PNAVGPGPSI PTQALGGGLG
     QGLLIDMKGG ELVFGPNPLT PEFSISGAPI ATLWVSVNGG APVAVPSIID SGGVMGTIPS
     SVIGGSTLPA NTNITVYTDN TMTTEVYHYS TNDYQPTVIS SGLMNTGFLP FWNQPVYIDY
     SPAGTGTTVF DMP