GRPE_MYCTU
ID GRPE_MYCTU Reviewed; 235 AA.
AC P9WMT5; L0T3E5; O08379; P32724;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Protein GrpE {ECO:0000255|HAMAP-Rule:MF_01151};
DE AltName: Full=HSP-70 cofactor {ECO:0000255|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000255|HAMAP-Rule:MF_01151}; OrderedLocusNames=Rv0351;
GN ORFNames=MTCY13E10.11;
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 [GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RA Lathigra R., Alexander B., Stover C.K., Coadwell J., Young R.A.,
RA Young D.B.;
RL Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Participates actively in the response to hyperosmotic and
CC heat shock by preventing the aggregation of stress-denatured proteins,
CC in association with DnaK and GrpE. It is the nucleotide exchange factor
CC for DnaK and may function as a thermosensor. Unfolded proteins bind
CC initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK
CC hydrolyzes its bound ATP, resulting in the formation of a stable
CC complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the
CC release of the substrate protein, thus completing the reaction cycle.
CC Several rounds of ATP-dependent interactions between DnaJ, DnaK and
CC GrpE are required for fully efficient folding. {ECO:0000255|HAMAP-
CC Rule:MF_01151}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP-
CC Rule:MF_01151}.
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DR EMBL; X58406; CAA41307.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43081.1; -; Genomic_DNA.
DR PIR; H70574; H70574.
DR RefSeq; NP_214865.1; NC_000962.3.
DR RefSeq; WP_003401817.1; NZ_NVQJ01000002.1.
DR AlphaFoldDB; P9WMT5; -.
DR SMR; P9WMT5; -.
DR STRING; 83332.Rv0351; -.
DR iPTMnet; P9WMT5; -.
DR PaxDb; P9WMT5; -.
DR DNASU; 886497; -.
DR GeneID; 45424317; -.
DR GeneID; 886497; -.
DR KEGG; mtu:Rv0351; -.
DR TubercuList; Rv0351; -.
DR eggNOG; COG0576; Bacteria.
DR OMA; LEGPFKA; -.
DR PhylomeDB; P9WMT5; -.
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:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IEP:MTBBASE.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 2.30.22.10; -; 1.
DR Gene3D; 3.90.20.20; -; 1.
DR HAMAP; MF_01151; GrpE; 1.
DR InterPro; IPR000740; GrpE.
DR InterPro; IPR013805; GrpE_coiled_coil.
DR InterPro; IPR009012; GrpE_head.
DR PANTHER; PTHR21237; PTHR21237; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF51064; SSF51064; 1.
DR SUPFAM; SSF58014; SSF58014; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..235
FT /note="Protein GrpE"
FT /id="PRO_0000113824"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CONFLICT 110
FT /note="D -> H (in Ref. 1; CAA41307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 24533 MW; 56838BA488B6AF21 CRC64;
MTDGNQKPDG NSGEQVTVTD KRRIDPETGE VRHVPPGDMP GGTAAADAAH TEDKVAELTA
DLQRVQADFA NYRKRALRDQ QAAADRAKAS VVSQLLGVLD DLERARKHGD LESGPLKSVA
DKLDSALTGL GLVAFGAEGE DFDPVLHEAV QHEGDGGQGS KPVIGTVMRQ GYQLGEQVLR
HALVGVVDTV VVDAAELESV DDGTAVADTA ENDQADQGNS ADTSGEQAES EPSGS
