ID   ESPG5_MYCMM             Reviewed;         300 AA.
AC   B2HSU5;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=ESX-5 secretion-associated protein EspG5 {ECO:0000305};
GN   Name=espG5 {ECO:0000303|PubMed:22843727};
GN   OrderedLocusNames=MMAR_2676 {ECO:0000312|EMBL:ACC41119.1};
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   FUNCTION, INTERACTION WITH PPE33, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=E11;
RX   PubMed=22843727; DOI=10.1074/jbc.m112.397596;
RA   Daleke M.H., van der Woude A.D., Parret A.H., Ummels R., de Groot A.M.,
RA   Watson D., Piersma S.R., Jimenez C.R., Luirink J., Bitter W., Houben E.N.;
RT   "Specific chaperones for the type VII protein secretion pathway.";
RL   J. Biol. Chem. 287:31939-31947(2012).
RN   [3]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=22925462; DOI=10.1111/j.1365-2958.2012.08206.x;
RA   Houben E.N., Bestebroer J., Ummels R., Wilson L., Piersma S.R.,
RA   Jimenez C.R., Ottenhoff T.H., Luirink J., Bitter W.;
RT   "Composition of the type VII secretion system membrane complex.";
RL   Mol. Microbiol. 86:472-484(2012).
CC   -!- FUNCTION: Specific chaperone for cognate PE/PPE proteins. Plays an
CC       important role in preventing aggregation of PE/PPE dimers. Required for
CC       LipY and PE31/PPE18 secretion. {ECO:0000269|PubMed:22843727}.
CC   -!- SUBUNIT: Interacts specifically with ESX-5-dependent PE/PPE proteins.
CC       Binds PPE33 and PPE18. Does not interact with EsxN. Monomer in
CC       solution. {ECO:0000269|PubMed:22843727}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22843727,
CC       ECO:0000269|PubMed:22925462}.
CC   -!- SIMILARITY: Belongs to the EspG family. {ECO:0000305}.
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DR   EMBL; CP000854; ACC41119.1; -; Genomic_DNA.
DR   RefSeq; WP_012394390.1; NC_010612.1.
DR   AlphaFoldDB; B2HSU5; -.
DR   SMR; B2HSU5; -.
DR   STRING; 216594.MMAR_2676; -.
DR   EnsemblBacteria; ACC41119; ACC41119; MMAR_2676.
DR   GeneID; 64261389; -.
DR   KEGG; mmi:MMAR_2676; -.
DR   eggNOG; ENOG5031DB5; Bacteria.
DR   HOGENOM; CLU_908572_0_0_11; -.
DR   OMA; TDNNDWL; -.
DR   OrthoDB; 1266830at2; -.
DR   PHI-base; PHI:3602; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR025734; EspG.
DR   Pfam; PF14011; ESX-1_EspG; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..300
FT                   /note="ESX-5 secretion-associated protein EspG5"
FT                   /id="PRO_0000435130"
SQ   SEQUENCE   300 AA;  32352 MW;  6505A2DC703E3F70 CRC64;
     MDQQSTRTDI TVNVDGFWML QALLDIRHVA PELRCRPYVS TDSNDWLNEH PGMAVMREQG
     IVVGDTVNEQ VAARMRVLAA PDLEVVALLS RGKLLYGVVD NEDQPPGSRD IPDNEFRVVL
     ARRGQHWVSA VRVGNDITVD DVSVSDSASI AALVIDGLES IHHADPAAIN AVNVPLEEML
     EATKSWQESG FNVFSGGDLR RMGISASTVA ALGQALSDPA AEVAVYARQY RDDAKGPSAS
     VLSLKDGSGG RIALYQQART AGSGEAWLAI CPATPQLVQV GVKTVLDTLP YGEWKTHSRV