ID   HTPG_PECAS              Reviewed;         627 AA.
AC   Q6D7Z6;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=ECA1179;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00505}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG74089.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX950851; CAG74089.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q6D7Z6; -.
DR   SMR; Q6D7Z6; -.
DR   STRING; 218491.ECA1179; -.
DR   EnsemblBacteria; CAG74089; CAG74089; ECA1179.
DR   KEGG; eca:ECA1179; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..627
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224207"
FT   REGION          1..339
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          340..555
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          556..627
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   627 AA;  71249 MW;  C4FF6574D977CE92 CRC64;
     MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSTPELYAGD
     GDLRVRVSTD KEKRTLTISD NGIGMSRDEV IDNLGTIAKS GTKSFLESMG SDQVKDSQLI
     GQFGVGFYSA FIVADKVTVR TRAAGANADQ GVYWESAGEG DYTIADITKD DRGTEITLHL
     REGEDEFLDD WRVRSVISKY SDHIALPVEI ESQTESEEEG GESTVSWEKI NKAQALWTRS
     KSEVSDDEYN EFYKHISHDF TDPLSWSHNR VEGKQEYTSL LYIPAHAPWD MWNRDHKHGL
     KLYVQRVFIM DDAEQFMPNY LRFVRGLIDS NDLPLNVSRE ILQDSRVTQN LRNALTKRVL
     QMLDKLAKDD AEKYQTFWQQ FGLVLKEGPA EDGSNREAIA KLLRFATTQS DSSAQTVSLE
     DYVSRMVEGQ DKIYYITADS YAAAKSSPHL ELFRKKGIEV LLLSERIDEW MMSYLTEFDG
     KSFQSVSKAD DTLDKLADEE NDAQKEAQKA LEPFVERVKT LLGERVKDVR FTYRLTDTPA
     IVVTDADEMS TQMAKLFAAA GQQAPEVKYI FELNPEHALI KRAADVSDEA EFGEWVELLL
     DQALLAERGT LDDPNLFIRR MNQLLSA