ID   ESPG1_MYCMM             Reviewed;         279 AA.
AC   B2HMS9;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=ESX-1 secretion-associated protein EspG1 {ECO:0000305};
GN   Name=espG1 {ECO:0000303|PubMed:22843727};
GN   OrderedLocusNames=MMAR_5441 {ECO:0000312|EMBL:ACC43848.1};
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, AND SUBUNIT.
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   SUBUNIT.
RX   PubMed=25155747; DOI=10.1111/mmi.12770;
RA   Korotkova N., Freire D., Phan T.H., Ummels R., Creekmore C.C., Evans T.J.,
RA   Wilmanns M., Bitter W., Parret A.H., Houben E.N., Korotkov K.V.;
RT   "Structure of the Mycobacterium tuberculosis type VII secretion system
RT   chaperone EspG5 in complex with PE25-PPE41 dimer.";
RL   Mol. Microbiol. 94:367-382(2014).
CC   -!- FUNCTION: Specific chaperone for cognate PE/PPE proteins
CC       (PubMed:22843727). Plays an important role in preventing aggregation of
CC       PE/PPE dimers (By similarity). {ECO:0000250|UniProtKB:O53943,
CC       ECO:0000269|PubMed:22843727}.
CC   -!- SUBUNIT: Interacts specifically with ESX-1-dependent PE/PPE proteins.
CC       {ECO:0000269|PubMed:22843727, ECO:0000269|PubMed:25155747}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B2HSU5}.
CC   -!- SIMILARITY: Belongs to the EspG family. {ECO:0000305}.
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DR   EMBL; CP000854; ACC43848.1; -; Genomic_DNA.
DR   RefSeq; WP_012396941.1; NC_010612.1.
DR   AlphaFoldDB; B2HMS9; -.
DR   SASBDB; B2HMS9; -.
DR   SMR; B2HMS9; -.
DR   STRING; 216594.MMAR_5441; -.
DR   EnsemblBacteria; ACC43848; ACC43848; MMAR_5441.
DR   KEGG; mmi:MMAR_5441; -.
DR   eggNOG; ENOG502ZNK2; Bacteria.
DR   HOGENOM; CLU_073321_1_0_11; -.
DR   OMA; TLEARWW; -.
DR   OrthoDB; 1266830at2; -.
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..279
FT                   /note="ESX-1 secretion-associated protein EspG1"
FT                   /id="PRO_0000435128"
SQ   SEQUENCE   279 AA;  29825 MW;  C0A474874382EDA6 CRC64;
     MTGPLATGRA GTGDDVVGVE VTIDGMLVIA DRLHLVDFPV TLGIRPNIPQ EDLREIVWDQ
     VARDLTAQGV LDHNGQPHPA VAAMVDTLSR ADRTLEGRWW RRDVGGVMVR FVVCRKGERH
     VIAVRDGDML VLQLVAPRVG LAGMVTAVLG TAEPANVEPL TGIASELGEC TNAAQLTRYG
     LTPTTARLYT EIVTNPKSWV EIVASERHPG GTTTHTKAAA GVLDSAHGRL VSLPRQVGGE
     LYGSFLPGTE QNLQRALDSL LELLPSGSWL DRADATARG