ID   HTPG_VESOH              Reviewed;         616 AA.
AC   A5CWV5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=COSY_0454;
OS   Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Vesicomyosocius.
OX   NCBI_TaxID=412965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HA;
RX   PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA   Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA   Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T.,
RA   Kato C., Kitagawa M., Kato I., Maruyama T.;
RT   "Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea
RT   clam, Calyptogena okutanii.";
RL   Curr. Biol. 17:881-886(2007).
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}.
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DR   EMBL; AP009247; BAF61573.1; -; Genomic_DNA.
DR   RefSeq; WP_011929843.1; NC_009465.1.
DR   AlphaFoldDB; A5CWV5; -.
DR   SMR; A5CWV5; -.
DR   STRING; 412965.COSY_0454; -.
DR   EnsemblBacteria; BAF61573; BAF61573; COSY_0454.
DR   KEGG; vok:COSY_0454; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000247; 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; 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; Stress response.
FT   CHAIN           1..616
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014963"
FT   REGION          1..334
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          335..549
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          550..616
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   616 AA;  70406 MW;  BB28F6C9EEBBBCB8 CRC64;
     MTIKQTHSFQ TEVSQLLHLM IHSLYSNKEI FLRELISNAS DAVDKLKFKS LSDDTLIEGK
     EALQIHIDVN KDANTITITD NGIGMSEVEV NKNIGTIANS GTKKFLKSLN ETQAQDSNLI
     GQFGVGFYSS FIVSDKVEII TRKAGSKSKK GTKWASTGKG KYSIESIDRP DFGTSVILHI
     KKDEKEFLDD YRLRNIISKY SDHITVPIMM VKVSEDNKDI EYERINKANA FWAQDKQDLK
     QKDYDEFYKS LTYDLEAPLT QLHNRVEGNI DYTSLLFIPS KSPFDIWEPK RKGGIKLYAK
     RVFIMEDNEA LMPLYLRFVK GVIDTADLSL NLSREILQDN KVIKAIRKAS VKRILSVLEK
     MAKNKPEDYA TFWQEFGMLM KEGVVEDTIN KDKIAKLLRF TTNKSKNATQ TVTLEHYIKN
     IQKDQKAIYY ITAETYETAK GSPHLENFNQ KNIEVLLLSD RVDEWMVSNF REFDGIQLKS
     IAKGNLEDFD SKEEKKAKEE VAKNFEIVIE KMQKILDSQV KEIKISSRLS ESPSCLVADE
     NEMGGNMERI MKSLGQDIPD TKPILEINPT HSLVKKLKTK IDEDLVKVLF DQAVLSEGGQ
     LKDPAEFVKR INKLIN