ID   HTPG_MARMS              Reviewed;         642 AA.
AC   A6VXW3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Mmwyl1_2370;
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1;
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., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-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; CP000749; ABR71292.1; -; Genomic_DNA.
DR   RefSeq; WP_012070071.1; NC_009654.1.
DR   AlphaFoldDB; A6VXW3; -.
DR   SMR; A6VXW3; -.
DR   STRING; 400668.Mmwyl1_2370; -.
DR   PRIDE; A6VXW3; -.
DR   EnsemblBacteria; ABR71292; ABR71292; Mmwyl1_2370.
DR   KEGG; mmw:Mmwyl1_2370; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
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..642
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081519"
FT   REGION          1..350
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          351..567
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          568..642
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   642 AA;  73088 MW;  02BC344B9EE4A8A4 CRC64;
     MATDTQKETL GFQTEVKQLL HLMIHSLYSN KEIFLRELIS NASDAVDKLR FESVANADLL
     AEDPNLRVRI EFDKDTNTVV IDDNGVGMSR EEAITNLGTI AKSGTSAFLE QLSGDQKKDS
     QLIGQFGVGF YSAFIVADKV TVETRRAGVA ADQAVRWVSD GSGEFTIENI EKDSRGTRII
     LHLKAGEKEF ADNFRLRHLV TKYSDHISIP VEMEKPVYPE MDEEGNPKPV DENKAPEYEA
     VNSAKALWTR PRNEVTDEEY QEFYKHISHD YQEPLKWSHN KVEGKLEYSS LLYIPSKAPY
     DLWNRDMQRG LKLYVQRVFI MDEAEAFLPP YMRFVKGVVD SNDLSLNVSR EILQNDHAVD
     SMRSALTKRV LDMLGKMAKN EPEDYQKFWD EFGNVIKEGP ADDMGNKDKI AGLLRFSSTH
     TDAAAQTVSL ADYIERMQEG QDKIYYIYAE SHNTAKNSPH LEILRKKGFE VLLLSDRIDE
     WMMSSLQEFE GKSFQDVTKG KLDLADQENE EEKKEKEEKA EKMKPLLDRM KAVLNEKVAG
     VNSTDRLTNS PACLVVGEYD MGLQMRRLLE QAGQKLPESK PTLEVNPDHP IVAKMDSETD
     EERFADMAWL LFEQATLSEG GQLEDPATFV SRMNKLIVQL SK