ID   HTPG_ALCBS              Reviewed;         615 AA.
AC   Q0VPG1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=ABO_1489;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL16937.1; -; Genomic_DNA.
DR   RefSeq; WP_011588770.1; NC_008260.1.
DR   AlphaFoldDB; Q0VPG1; -.
DR   SMR; Q0VPG1; -.
DR   STRING; 393595.ABO_1489; -.
DR   EnsemblBacteria; CAL16937; CAL16937; ABO_1489.
DR   KEGG; abo:ABO_1489; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000008871; 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; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..615
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258502"
FT   REGION          1..335
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          336..541
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          542..615
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   615 AA;  68889 MW;  5261A98DBC4999D4 CRC64;
     MSAEKQTHGF QAEVSRLLHL MIHSLYSNRE IFLRELISNA SDACDKLRFE ALDNPALLEQ
     GGEPQITLRV DKDAGTLTIA DNGIGMSENE VVDNLGTIAR SGTEKFLANL SGDQKKDAQL
     IGQFGVGFYS AFIVAETVTV ETRKAGEAVN NGVRWESDGK GEFTVETVPR DEQGTAVILH
     LRDDAKDFLD DFKIRQVIGQ YSDHVAFPIV LETPQEGDKD TKTETLNSAT ALWQRPRSEV
     TDEEYQSFYK HISHDFQDAL TWSHNKVEGK LEYTSLLYVP AQAPFDLYQR EANRGLKLYV
     QRVFIMDDAE QFLPQYLRFI KGVIDAPDLP LNVSRELLQD YGPVQKIRSA LTKRVLQMLK
     KLSNDDKQYA KFWAQFGSVI KEGVAEDRDN QQSIAALLRF ATSKTPDSVS TSLDQYLESK
     PADQDCIYYL LADTPSAARQ SPHLEVFRKK GIEVLLLSDP VDEWMVGYLE SYKEVKLVNA
     ARGELDLGDE SEQANNDDPL IQRLAASLTE QVEAVRATTR LVDSPACLVL AEDQLGPQMR
     RMLEAAGQPV PENKPVLEVN LDHTLLQALT RIEEDEKFND FAALLLDQAM LAEGQLPKDP
     AATARRMQAL LSQSV