ID   HTPG_ALIB4              Reviewed;         636 AA.
AC   A8EV23;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-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=Abu_1547;
OS   Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Aliarcobacter.
OX   NCBI_TaxID=367737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM4018;
RX   PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA   Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA   Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA   Rogosin A., Stanker L.H., Mandrell R.E.;
RT   "The complete genome sequence and analysis of the Epsilonproteobacterium
RT   Arcobacter butzleri.";
RL   PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV67796.1; -; Genomic_DNA.
DR   RefSeq; WP_012013180.1; NC_009850.1.
DR   AlphaFoldDB; A8EV23; -.
DR   SMR; A8EV23; -.
DR   STRING; 367737.Abu_1547; -.
DR   EnsemblBacteria; ABV67796; ABV67796; Abu_1547.
DR   KEGG; abu:Abu_1547; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001136; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..636
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000060524"
FT   REGION          1..349
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          350..562
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          563..636
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   636 AA;  72152 MW;  7E582FDCFE13A256 CRC64;
     MAKHQFQTEV GQLLHLMTHS LYSNKEIFIR ELVSNASDAI DKLNYLRLTD ENLKDKYAQW
     KGEINISFDE KDKSLSIIDN GIGMNEADLI ASIGTIAKSG TKSFVEALTG DAKKDSNLIG
     QFGVGFYSVF MVADKVDVIS KKAGEEQAYK WSSTGTGEFD LTPCTKESNG TVIYIKLKDE
     EAGEFASKYR IKNIVEKYSN HIAYPIFLNY DEEVSEALSE EDEKAGKKPE KKIERKHEQI
     NAATALWMQP KAKLKEQDYN DFYKSISHDS SDPMLTIHTK TEGVNEYTTL FYIPKIAPMD
     MYRADFQSGV KLYVKRVFIT DDEKELLPTY LRFVRGIIDS EDLPLNVSRE ILQENRILAN
     IKQGSVKKIL AEIKKLSKDE EKYAEFVAQY IRPLKEGVYQ DYTNKEAILE LLRYKSSKTE
     AGKMTSLEAY KERANSEQKA IYYIVGENEK VLRNSPLLES YKKNDIEVLI LDDKEIDEII
     TPAIGAFKEW EFKDITAIEP PKVEQSEEEK KEVEEKFQDI LSKIKDKLGD AVKDVKVTSR
     LSESPSCVVK DAADAQMAAM AHMFRAMGQA MPESAPILEI NPEHEIVKKL NGCADEATIE
     DVSWILLDQA KLSEGMEITD TVAFAQRLSR ITAKAL