ID   HTPG_SALAI              Reviewed;         636 AA.
AC   A8M4S6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Sare_2657;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000850; ABV98494.1; -; Genomic_DNA.
DR   RefSeq; WP_012182795.1; NC_009953.1.
DR   AlphaFoldDB; A8M4S6; -.
DR   SMR; A8M4S6; -.
DR   STRING; 391037.Sare_2657; -.
DR   EnsemblBacteria; ABV98494; ABV98494; Sare_2657.
DR   GeneID; 5703578; -.
DR   KEGG; saq:Sare_2657; -.
DR   PATRIC; fig|391037.6.peg.2692; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_11; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
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; Stress response.
FT   CHAIN           1..636
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081523"
FT   REGION          1..342
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          343..558
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          559..636
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   636 AA;  71470 MW;  61AE4D8614BB457D CRC64;
     MSGETLEFQA EARQLLQLMV HSIYSNKDVF LRELISNASD ALDKLRLASM RDKDLDVDTS
     DLHIAIEVDQ DARTLTVRDN GIGMTRDEVV QVIGTIAKSG TAELLRKLRE TTDAETSQEL
     IGQFGVGFYA AFMVADRVVL VTRQAGEADG THWESSGEGT YTIAPATDVP QGTAVTLHLK
     PVDSEDNLHD YAAEWTIRQI VKRYSDFIAH PIRMAVERPG SDDSEPTTEV QTLNSMKALW
     ARPRDEVEPA EYHEFYKHVS HDWADPLEVV HMRGEGTFEY EALLFLPTHA PLDLFSPQGR
     RGVQLYVKRV FIMDDCEALM PGYLRFVKGV VDAHDLSLNI SRELLQQDRQ IQVVRRRLVK
     KVLATVKDLK ANQPEKYRTF WTEFGAVVKE GLIDDTENRD SLLEILSVAS THDPAEPTDL
     TGYVNRMKDG QSEIYYATGE NRTTIENSPH MEAFRAKGFE VLLLTDPVDE VWVERVGEYD
     GKTLRSVAKG QVDLDTDEER SAAEAERERQ RTEYADLLTW LGSALADQVR EVRLSARLTT
     SPACVVGDAH DVTPTLEKMY RAMGHEVPQV KRILELNPTH PLVSGLRKAR EQGATEDSLT
     ETAELLYGMA LLAEGGELAD PSRFTRILAE RLARTL