HTPG_MARN8
ID HTPG_MARN8 Reviewed; 630 AA.
AC A1TZH7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=Maqu_1054;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM18146.1; -; Genomic_DNA.
DR RefSeq; WP_011784564.1; NC_008740.1.
DR AlphaFoldDB; A1TZH7; -.
DR SMR; A1TZH7; -.
DR STRING; 351348.Maqu_1054; -.
DR PRIDE; A1TZH7; -.
DR EnsemblBacteria; ABM18146; ABM18146; Maqu_1054.
DR KEGG; maq:Maqu_1054; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000000998; 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..630
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014928"
FT REGION 1..338
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 339..555
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 556..630
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 630 AA; 71534 MW; 0A73257B469E7FE8 CRC64;
MTVEANKETL GFQTEVKQLL HLMIHSLYSN KEIFLRELIS NASDAEDKLR FAALKDDKLF
EGDSDLKIRL DYDKDAGTIT IADNGIGMTR DDVIANLGTI AKSGTAEFLK QLSGDEKKDS
KLIGQFGVGF YSAFIVADKV EVFTRKAGEP ADNGVHWESK GDGEFTIEPV SREQRGTEIV
LHLKPEDKEF ADGWKLRSLV KKYSDHISFP VVMKSESEEE DKKGEEETVN DATALWTLPR
TEIKDEEYKE FYKHIAHDFE DPLTWSHNKV EGKLDYTSLL YIPKRAPFDL YNREAPRGLK
LYVQRVFIMD DAEQFLPLYL RFTKGVIDSN DLSLNVSREI LQNDSTVESI RTALTKRVLD
MLSKLAKKGG DEYQGFWDEF GTVLKEGPAE DFSNREKIAG LLRFASTHTG EATQNVSLDD
YISRMKEGQN KIYYITGDNF AAAKSSPHLE VFRKKGIEVL ILSDRIDEWM MGYLSEYDGK
QFQDVARGDL DLGEVETEED KKHQEEAAKE HKDLLERIKT ALEDQVQEVR VTNRLTDSPA
CLVVGQFDMG AQMKKIMEAA GQKVPESKPI FEINVDHPLV QRLETEQGEQ RFKELSAVLF
DQATLASGEQ LKDPGAYVSR LNRLLLELAN