ID   HTPG_MYXXD              Reviewed;         654 AA.
AC   Q1CZI7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=MXAN_6051;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF89090.1; -; Genomic_DNA.
DR   RefSeq; WP_011556000.1; NC_008095.1.
DR   AlphaFoldDB; Q1CZI7; -.
DR   SMR; Q1CZI7; -.
DR   STRING; 246197.MXAN_6051; -.
DR   EnsemblBacteria; ABF89090; ABF89090; MXAN_6051.
DR   GeneID; 41363289; -.
DR   KEGG; mxa:MXAN_6051; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002402; 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..654
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258515"
FT   REGION          1..344
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          345..556
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          557..654
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   654 AA;  73272 MW;  6F64A7ADA83AD31C CRC64;
     MTVENAPQRE THAFQAEINQ LLSLVINSLY SHKEIFLREL VSNASDALDK LRFRAITEPE
     LLADEPALEL RLIPDEAKGT LTIEDTGIGM SHDELVKNLG TIAHSGSREF IEALAQKGQQ
     KDMQLIGQFG VGFYSAYLVA DRVEVVSRAA GQGQSAWRWT SEAKGSFTVE PAERAARGTS
     ITLHLKEDQK EFLGEWRLRS LITQYSDYVG HPIKLQVSKT TGTGDEAKTE TSLEVVNKAS
     ALWQRSKSEI TDEQYQEFYK HLTHDWEAPL AWTHFKADGN TQFTGLLFVP KQPPFDLDAQ
     QQRGVRLFVK RVFIMDRCEE LVPQWLRFVR GVIDSDDLPL NVSRELLQDS QVVRAIRKHV
     VKKSVDLLEK LAKDKPDDYL TFWKAFGTVL KEGLATEAEQ KDKLGGLLRY ESSREEGLTS
     LADYVGRMKE GQEAIYYVYG ESRKAVADSP HLEALKQRGF EVLYMTDPVD EWAAQGLREF
     QGKPLVSALQ ADLKLQSTDE QKKEQEQHAE GLKTLTSKMK DVLQESVREV RVSDRLTDSP
     VCLVVPEGGS PAYLERLLQQ RGRGAGMPRV KRILEVNPKH PVIEHLKAVH DRDPAAAQVA
     EWIELLHDQA LLTEGSTIAD PNRFARRMTG LLTQVAALAA APAPAQTPAS ATAS