ESPG5_MYCTU
ID ESPG5_MYCTU Reviewed; 300 AA.
AC O53943; F2GIW9; I6XZ10; Q7D7Y5;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ESX-5 secretion-associated protein EspG5 {ECO:0000305};
GN Name=espG5 {ECO:0000303|PubMed:25155747};
GN OrderedLocusNames=Rv1794 {ECO:0000312|EMBL:CCP44560.1};
GN ORFNames=LH57_09810 {ECO:0000312|EMBL:AIR14543.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=22340629; DOI=10.1111/j.1365-2958.2012.08001.x;
RA Bottai D., Di Luca M., Majlessi L., Frigui W., Simeone R., Sayes F.,
RA Bitter W., Brennan M.J., Leclerc C., Batoni G., Campa M., Brosch R.,
RA Esin S.;
RT "Disruption of the ESX-5 system of Mycobacterium tuberculosis causes loss
RT of PPE protein secretion, reduction of cell wall integrity and strong
RT attenuation.";
RL Mol. Microbiol. 83:1195-1209(2012).
RN [5] {ECO:0007744|PDB:4KXR}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH PE25 AND PPE41,
RP FUNCTION, AND 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).
RN [6] {ECO:0007744|PDB:4W4L}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH PE25 AND PPE41.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=25275011; DOI=10.1073/pnas.1409345111;
RA Ekiert D.C., Cox J.S.;
RT "Structure of a PE-PPE-EspG complex from Mycobacterium tuberculosis reveals
RT molecular specificity of ESX protein secretion.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:14758-14763(2014).
CC -!- FUNCTION: Specific chaperone for cognate PE/PPE proteins. Plays an
CC important role in preventing aggregation of PE/PPE dimers.
CC {ECO:0000269|PubMed:25155747}.
CC -!- SUBUNIT: Interacts specifically with ESX-5-dependent PE/PPE proteins.
CC Forms a 1:1:1 heterotrimeric complex with the PE25/PPE41 dimer, via
CC PPE41. Binding of EspG5 does not cause conformational changes in the
CC PE25/PPE41 dimer. {ECO:0000269|PubMed:25155747,
CC ECO:0000269|PubMed:25275011}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B2HSU5}.
CC -!- DISRUPTION PHENOTYPE: Deletion does not affect EsxN and PPE41
CC secretion. {ECO:0000269|PubMed:22340629}.
CC -!- SIMILARITY: Belongs to the EspG family. {ECO:0000305}.
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DR EMBL; CP009480; AIR14543.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44560.1; -; Genomic_DNA.
DR RefSeq; NP_216310.1; NC_000962.3.
DR RefSeq; WP_003408846.1; NZ_NVQJ01000037.1.
DR PDB; 4KXR; X-ray; 2.60 A; C=1-300.
DR PDB; 4W4L; X-ray; 2.45 A; C=1-300.
DR PDB; 5XFS; X-ray; 2.90 A; C=1-300.
DR PDBsum; 4KXR; -.
DR PDBsum; 4W4L; -.
DR PDBsum; 5XFS; -.
DR AlphaFoldDB; O53943; -.
DR SASBDB; O53943; -.
DR SMR; O53943; -.
DR STRING; 83332.Rv1794; -.
DR TCDB; 3.A.24.4.1; the type vii or esx protein secretion system (t7ss) family.
DR PaxDb; O53943; -.
DR PRIDE; O53943; -.
DR DNASU; 885881; -.
DR GeneID; 45425771; -.
DR GeneID; 885881; -.
DR KEGG; mtu:Rv1794; -.
DR PATRIC; fig|83332.111.peg.1999; -.
DR TubercuList; Rv1794; -.
DR eggNOG; ENOG5031DB5; Bacteria.
DR HOGENOM; CLU_908572_0_0_11; -.
DR OMA; TDNNDWL; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR InterPro; IPR025734; EspG.
DR Pfam; PF14011; ESX-1_EspG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..300
FT /note="ESX-5 secretion-associated protein EspG5"
FT /id="PRO_0000435131"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:4KXR"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:4KXR"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:4KXR"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4KXR"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 82..93
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:4KXR"
FT HELIX 147..161
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4KXR"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:4KXR"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:4KXR"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:4KXR"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:4KXR"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 220..231
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:4KXR"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:4KXR"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:5XFS"
SQ SEQUENCE 300 AA; 32400 MW; 48937E99E6742E6E CRC64;
MDQQSTRTDI TVNVDGFWML QALLDIRHVA PELRCRPYVS TDSNDWLNEH PGMAVMREQG
IVVNDAVNEQ VAARMKVLAA PDLEVVALLS RGKLLYGVID DENQPPGSRD IPDNEFRVVL
ARRGQHWVSA VRVGNDITVD DVTVSDSASI AALVMDGLES IHHADPAAIN AVNVPMEEML
EATKSWQESG FNVFSGGDLR RMGISAATVA ALGQALSDPA AEVAVYARQY RDDAKGPSAS
VLSLKDGSGG RIALYQQART AGSGEAWLAI CPATPQLVQV GVKTVLDTLP YGEWKTHSRV
