ID   HTPG_ALKMQ              Reviewed;         626 AA.
AC   A6TKN0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=Amet_0521;
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF;
RX   PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA   Hwang C., 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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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; CP000724; ABR46748.1; -; Genomic_DNA.
DR   RefSeq; WP_011971656.1; NC_009633.1.
DR   AlphaFoldDB; A6TKN0; -.
DR   SMR; A6TKN0; -.
DR   STRING; 293826.Amet_0521; -.
DR   EnsemblBacteria; ABR46748; ABR46748; Amet_0521.
DR   KEGG; amt:Amet_0521; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_9; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001572; 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; 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; 2.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
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..626
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000060522"
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          342..552
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          553..626
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   626 AA;  72971 MW;  1603269366AD8F95 CRC64;
     MIKKEFKAES KRLLDLMINS IYTHKEIFLR ELISNSSDAI DKIYYKALTD ESMIFNKEDY
     YIKITTDKEN KMLIISDMGI GMTKEELEEN LGVIAQSGSF TFKKENEIKD GFDIIGQFGV
     GFYSAFMVAD SVTVISKALG SDQGYKWESI GAEGYTIEPY EKESVGTEII LKLKENTEDE
     KYEDYLEAYR LKTIIKKYSD FIRYPIKMDI ETSKPKEGAE GEYEEIVEEQ VVNSMVPMWR
     RNKNELTKED YDLFYSEKHY GFDKPLKHIH ISADGAVRYN AILFIPEKIP YDFYTKEYEK
     GLELYSSGVL IMNKCSDLLP DYFSFVKGMV DSEDLSLNIS REMLQHDRQL KIIAKKIKEK
     IKSELELLLK NERERYEEFY DSFGRQIKYG VYSDFGQNKE TLKDLLLFYS SKEKKMVTLD
     EYVGRMKEDQ KYIYYASGDS IEKIDKMPQT ELLAEQGYEI LYFADDVDEF AIRVLVDYKE
     KEFKSVSSGD LGIEEKDEKE EQEEQTQGSK EVFAFMKEAL SQKVKDVRPS KRLKNHPVCL
     ATDGDVTIEM EKILSAMPNN QEIKAERVLE ININHDVFKT LKEAFDNDQE KLKIYTNVLY
     NQALLIEGLT INDPVEFTND ICKLMS