HTPG_ECOLI
ID HTPG_ECOLI Reviewed; 624 AA.
AC P0A6Z3; P10413; Q2MBV4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Chaperone protein HtpG;
DE AltName: Full=Heat shock protein C62.5;
DE AltName: Full=Heat shock protein HtpG;
DE AltName: Full=High temperature protein G;
GN Name=htpG; OrderedLocusNames=b0473, JW0462;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3299380; DOI=10.1073/pnas.84.15.5177;
RA Bardwell J.C.A., Craig E.A.;
RT "Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia
RT coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5177-5181(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-11.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP PROTEIN SEQUENCE OF 1-8, SUBUNIT, AND PHOSPHORYLATION.
RX PubMed=2647735; DOI=10.1016/s0021-9258(18)83755-3;
RA Spence J., Georgopoulos C.;
RT "Purification and properties of the Escherichia coli heat shock protein,
RT HtpG.";
RL J. Biol. Chem. 264:4398-4403(1989).
RN [7]
RP ATPASE ACTIVITY.
RX PubMed=8419347; DOI=10.1016/s0021-9258(18)54100-4;
RA Nadeau K., Das A., Walsh C.T.;
RT "Hsp90 chaperonins possess ATPase activity and bind heat shock
RT transcription factors and peptidyl prolyl isomerases.";
RL J. Biol. Chem. 268:1479-1487(1993).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP DOMAIN STRUCTURE.
RX PubMed=11606187; DOI=10.1046/j.0014-2956.2001.02457.x;
RA Nemoto T.K., Ono T., Kobayakawa T., Tanaka E., Baba T.T., Tanaka K.,
RA Takagi T., Gotoh T.;
RT "Domain-domain interactions of HtpG, an Escherichia coli homologue of
RT eukaryotic HSP90 molecular chaperone.";
RL Eur. J. Biochem. 268:5258-5269(2001).
RN [10]
RP DOMAIN STRUCTURE.
RX PubMed=11237871; DOI=10.1042/0264-6021:3540663;
RA Nemoto T.K., Ono T., Tanaka K.;
RT "Substrate-binding characteristics of proteins in the 90 kDa heat shock
RT protein family.";
RL Biochem. J. 354:663-670(2001).
RN [11]
RP SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 511-624, AND HOMODIMERIZATION.
RX PubMed=15274928; DOI=10.1016/j.str.2004.03.020;
RA Harris S.F., Shiau A.K., Agard D.A.;
RT "The crystal structure of the carboxy-terminal dimerization domain of htpG,
RT the Escherichia coli Hsp90, reveals a potential substrate binding site.";
RL Structure 12:1087-1097(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-559 IN COMPLEX WITH ATP, AND
RP CATALYTIC ACTIVITY.
RX PubMed=15837196; DOI=10.1016/j.str.2004.12.018;
RA Huai Q., Wang H., Liu Y., Kim H.Y., Toft D., Ke H.;
RT "Structures of the N-terminal and middle domains of E. coli Hsp90 and
RT conformation changes upon ADP binding.";
RL Structure 13:579-590(2005).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ADP.
RX PubMed=17055434; DOI=10.1016/j.cell.2006.09.027;
RA Shiau A.K., Harris S.F., Southworth D.R., Agard D.A.;
RT "Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent
RT conformational rearrangements.";
RL Cell 127:329-340(2006).
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity.
CC -!- SUBUNIT: Homodimer. Oligomerizes at 65 degrees Celsius.
CC {ECO:0000269|PubMed:15837196, ECO:0000269|PubMed:17055434,
CC ECO:0000269|PubMed:2647735}.
CC -!- INTERACTION:
CC P0A6Z3; P76236: cdgI; NbExp=3; IntAct=EBI-369221, EBI-552525;
CC P0A6Z3; P0A6Y8: dnaK; NbExp=3; IntAct=EBI-369221, EBI-542092;
CC P0A6Z3; P0A6Z3: htpG; NbExp=6; IntAct=EBI-369221, EBI-369221;
CC P0A6Z3; P0A8T7: rpoC; NbExp=3; IntAct=EBI-369221, EBI-543604;
CC P0A6Z3; P75862: zapC; NbExp=3; IntAct=EBI-369221, EBI-552519;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell
CC inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane
CC protein {ECO:0000269|PubMed:16079137}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:2647735}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; M38777; AAA23460.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40227.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73575.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76252.1; -; Genomic_DNA.
DR PIR; A28324; HHEC62.
DR RefSeq; NP_415006.1; NC_000913.3.
DR RefSeq; WP_000678201.1; NZ_SSZK01000009.1.
DR PDB; 1SF8; X-ray; 2.60 A; A/B/C/D/E/F/G/H=511-624.
DR PDB; 1Y4S; X-ray; 2.90 A; A/B=1-559.
DR PDB; 1Y4U; X-ray; 2.90 A; A/B=1-559.
DR PDB; 2GQ0; X-ray; 1.90 A; A/B=230-495.
DR PDB; 2IOP; X-ray; 3.55 A; A/B/C/D=1-624.
DR PDB; 2IOQ; X-ray; 3.50 A; A/B=1-624.
DR PDB; 2IOR; X-ray; 1.65 A; A=1-215.
DR PDBsum; 1SF8; -.
DR PDBsum; 1Y4S; -.
DR PDBsum; 1Y4U; -.
DR PDBsum; 2GQ0; -.
DR PDBsum; 2IOP; -.
DR PDBsum; 2IOQ; -.
DR PDBsum; 2IOR; -.
DR AlphaFoldDB; P0A6Z3; -.
DR SMR; P0A6Z3; -.
DR BioGRID; 4261971; 211.
DR BioGRID; 849488; 3.
DR DIP; DIP-29797N; -.
DR IntAct; P0A6Z3; 62.
DR STRING; 511145.b0473; -.
DR CarbonylDB; P0A6Z3; -.
DR SWISS-2DPAGE; P0A6Z3; -.
DR jPOST; P0A6Z3; -.
DR PaxDb; P0A6Z3; -.
DR PRIDE; P0A6Z3; -.
DR EnsemblBacteria; AAC73575; AAC73575; b0473.
DR EnsemblBacteria; BAE76252; BAE76252; BAE76252.
DR GeneID; 67416452; -.
DR GeneID; 945099; -.
DR KEGG; ecj:JW0462; -.
DR KEGG; eco:b0473; -.
DR PATRIC; fig|1411691.4.peg.1803; -.
DR EchoBASE; EB0456; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR InParanoid; P0A6Z3; -.
DR OMA; MRRMKEM; -.
DR PhylomeDB; P0A6Z3; -.
DR BioCyc; EcoCyc:EG10461-MON; -.
DR BioCyc; MetaCyc:EG10461-MON; -.
DR EvolutionaryTrace; P0A6Z3; -.
DR PHI-base; PHI:6472; -.
DR PRO; PR:P0A6Z3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:CACAO.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044183; F:protein folding chaperone; IDA:EcoCyc.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IMP:EcoCyc.
DR GO; GO:0006457; P:protein folding; IMP:EcoCyc.
DR GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Chaperone;
KW Cytoplasm; Direct protein sequencing; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..624
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000062985"
FT REGION 1..336
FT /note="A; substrate-binding"
FT REGION 337..552
FT /note="B"
FT REGION 553..624
FT /note="C"
FT REGION 585..624
FT /note="Mediates dimerization"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15837196"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15837196"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15837196"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15837196"
FT BINDING 255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15837196"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2IOR"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:2IOR"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:2IOR"
FT HELIX 30..50
FT /evidence="ECO:0007829|PDB:2IOR"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:2IOR"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2IOR"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:2IOR"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2IOR"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:2IOR"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:2IOR"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:2IOR"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:2IOR"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:2IOR"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1Y4S"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2IOR"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:2IOR"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:2IOR"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:2IOR"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:2IOR"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:2IOR"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2IOR"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1Y4S"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:2GQ0"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:2GQ0"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2GQ0"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:2GQ0"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:2GQ0"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:2GQ0"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:2GQ0"
FT STRAND 322..330
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 343..366
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 368..382
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:2GQ0"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:2GQ0"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 416..421
FT /evidence="ECO:0007829|PDB:2GQ0"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 438..442
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 448..453
FT /evidence="ECO:0007829|PDB:2GQ0"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:2GQ0"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:2GQ0"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:1Y4U"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 488..493
FT /evidence="ECO:0007829|PDB:2GQ0"
FT HELIX 511..519
FT /evidence="ECO:0007829|PDB:1SF8"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:1SF8"
FT STRAND 523..528
FT /evidence="ECO:0007829|PDB:1SF8"
FT STRAND 537..540
FT /evidence="ECO:0007829|PDB:1SF8"
FT HELIX 548..555
FT /evidence="ECO:0007829|PDB:1SF8"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:1SF8"
FT STRAND 567..570
FT /evidence="ECO:0007829|PDB:1SF8"
FT HELIX 575..582
FT /evidence="ECO:0007829|PDB:1SF8"
FT HELIX 586..605
FT /evidence="ECO:0007829|PDB:1SF8"
FT HELIX 611..623
FT /evidence="ECO:0007829|PDB:1SF8"
SQ SEQUENCE 624 AA; 71423 MW; 1410577B589ADBAD CRC64;
MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSNPDLYEGD
GELRVRVSFD KDKRTLTISD NGVGMTRDEV IDHLGTIAKS GTKSFLESLG SDQAKDSQLI
GQFGVGFYSA FIVADKVTVR TRAAGEKPEN GVFWESAGEG EYTVADITKE DRGTEITLHL
REGEDEFLDD WRVRSIISKY SDHIALPVEI EKREEKDGET VISWEKINKA QALWTRNKSE
ITDEEYKEFY KHIAHDFNDP LTWSHNRVEG KQEYTSLLYI PSQAPWDMWN RDHKHGLKLY
VQRVFIMDDA EQFMPNYLRF VRGLIDSSDL PLNVSREILQ DSTVTRNLRN ALTKRVLQML
EKLAKDDAEK YQTFWQQFGL VLKEGPAEDF ANQEAIAKLL RFASTHTDSS AQTVSLEDYV
SRMKEGQEKI YYITADSYAA AKSSPHLELL RKKGIEVLLL SDRIDEWMMN YLTEFDGKPF
QSVSKVDESL EKLADEVDES AKEAEKALTP FIDRVKALLG ERVKDVRLTH RLTDTPAIVS
TDADEMSTQM AKLFAAAGQK VPEVKYIFEL NPDHVLVKRA ADTEDEAKFS EWVELLLDQA
LLAERGTLED PNLFIRRMNQ LLVS
