ID   HTPG_METFK              Reviewed;         628 AA.
AC   Q1H2K2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=htpG1 {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=Mfla_0873;
GN   and
GN   Name=htpG2 {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=Mfla_1017;
OS   Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=265072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT / ATCC 51484 / DSM 6875;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT   "Complete sequence of Methylobacillus flagellatus KT.";
RL   Submitted (MAR-2006) 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; CP000284; ABE49285.1; -; Genomic_DNA.
DR   EMBL; CP000284; ABE49141.1; -; Genomic_DNA.
DR   RefSeq; WP_011479238.1; NC_007947.1.
DR   AlphaFoldDB; Q1H2K2; -.
DR   SMR; Q1H2K2; -.
DR   STRING; 265072.Mfla_0873; -.
DR   PRIDE; Q1H2K2; -.
DR   EnsemblBacteria; ABE49141; ABE49141; Mfla_0873.
DR   EnsemblBacteria; ABE49285; ABE49285; Mfla_1017.
DR   KEGG; mfa:Mfla_0873; -.
DR   KEGG; mfa:Mfla_1017; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002440; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..628
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258514"
FT   REGION          1..340
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          341..557
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          558..628
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   628 AA;  71062 MW;  8868E87F95617A82 CRC64;
     MSTETLQKET LGFQAEVKQL LQLMIHSLYS NKEIVLRELI SNASDAADKL RFEALADNSL
     YGNDSDLKIR VSFDKQARTI TISDNGIGMS REEVINNIGT IAKSGTKEFL QSLTGDQAKD
     ANLIGQFGVG FYSAFIIADK VTLTTRRAGS NEAVRWESTG EGDYTLEPAE KESRGTDIVL
     HLREGEDEFL NDWKLKSIIR KYSDHITLPI VMKKSEWKDG EQVPTDEDET VNKASALWAR
     NKSDISEQEY QEFYKHVSHD FENPLTWSHN RVEGKQEYIS LLYIPSKAPF DLYDRERQHG
     IKLYVKRVFI MDDAEQLMPQ YLRFVRGVID SADLPLNVSR EILQHSKDIE AIKTASVKRV
     LSMLEDLAEN KPEEYAKFWK EFGRVLKEGP GEDFANKERI AGLLRFASTH ADTDEQVVSF
     KDYIARMKEG QEAIYYITAD SFAAAKHSPH LEIFRKKGIE VLLLSDRVDE WLVSSLTEFD
     GKKLQSVAKG DLDLGKLEDE AEKEQQKKTE DEYKPLVERI QAALGDSVKE VRVTHRLTDS
     PACLVAGEHD LSGNLERLLK AAGQKTPGSK PILEINPDHG IVQRLKDVTD EAKFADWAHL
     LFDQALLAEG GQLEDPAAFV RRVNAMLA