HTPG_SHEB8
ID HTPG_SHEB8 Reviewed; 637 AA.
AC A6WPI2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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};
GN OrderedLocusNames=Shew185_2586;
OS Shewanella baltica (strain OS185).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=402882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS185;
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., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS185.";
RL Submitted (JUL-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; CP000753; ABS08721.1; -; Genomic_DNA.
DR RefSeq; WP_006086212.1; NC_009665.1.
DR AlphaFoldDB; A6WPI2; -.
DR SMR; A6WPI2; -.
DR GeneID; 11772753; -.
DR KEGG; sbm:Shew185_2586; -.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
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..637
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014952"
FT REGION 1..345
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 346..562
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 563..637
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 637 AA; 71663 MW; ABF129F430F73C28 CRC64;
MSQQETHGFQ TEVKQLLHLM IHSLYSNKEI FLRELVSNAA DAADKLRYLA LTNDALYEGD
GELRVRISAD KEKGTVTIED NGVGMTRDGV IEHLGTIAKS GTADFFKNLS GESSKDSQLI
GQFGVGFYSA FIVAKKVTVR TRAAGHKADE AVLWESEGEG NFTVDTITKA SRGTEITLHL
RDEEKEFADD WRLRSIITKY SDHISVPVEM WQEGTPESDG ADGEKIPATE GQWKVMNKAT
ALWMRSKADI SDEEYQEFYK HISHDYTDAL LWSHNRVEGK QEYTNLLYIP AKAPWDMWNR
DRKHGLKLFV QRVFIMDDAE QFMPSYLRFV QGLIDSNDLP LNVSREILQD NHVTKAMRTG
ITKRVLGMLE KLAKDDAEKY QQFWAEFGQV LKEGPAEDFA NRERIAGLLR FASTHTGSAA
PTVSLDDYIS RMKEGQTKIY YIVADSHEAA ANSPHLELLR KKGIEVLLMS ERIDEWLINH
LTEYKEKQLH SVTRGDLELG ELEDASEKEA QEKLEQESVA LVERIKAALG STVADVKVTS
RLTDTPACVV AGEGEMSTQM IKLMQAAGQP VPEVKPTFEI NPAHPLVSRL NDLQDEAAFA
DWSNLLLQQA QLSEKGSLAD PSAFIKLMNQ MLLANMK