ID   HTPG_ACTSZ              Reviewed;         628 AA.
AC   A6VML2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Asuc_0839;
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
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; CP000746; ABR74209.1; -; Genomic_DNA.
DR   RefSeq; WP_012072587.1; NC_009655.1.
DR   AlphaFoldDB; A6VML2; -.
DR   SMR; A6VML2; -.
DR   STRING; 339671.Asuc_0839; -.
DR   EnsemblBacteria; ABR74209; ABR74209; Asuc_0839.
DR   KEGG; asu:Asuc_0839; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001114; 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..628
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081512"
FT   REGION          1..339
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          340..556
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          557..628
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   628 AA;  71318 MW;  FE57255AD2000653 CRC64;
     MSNNQQTLGF QTEVKQLLQL MIHSLYSNKE IFLRELISNA SDAADKLRFK ALSAPELYEG
     DGDLKVRIRF DEKKGTLTVS DNGIGMTREQ ATEHLGTIAK SGTKEFLTAL GQDQAKDSQL
     IGQFGVGFYS AFIVADKVEV RSRAAGVPAE QGVLWTSAGE GEYSVEDIEK KERGTEITLF
     LREDEKEFLN EWRLREIIGK YSDHIGLPVE ILTKEFDEEG KESDVKWEKI NKAQALWTRA
     KGEISDEEYQ EFYKHISHDF ADPLVWQHNK VEGNQEYTSL LYVPSKAPWD LFNREQKHGL
     KLYVQRVFIM DDAEVFMPNY LRFMRGLLDS NDLPLNVSRE ILQDNKTTAA LRKALTKRSL
     QMLEKLAKDE AEKYATFWKE FGLVLKEGVG EDFANREQIA KLFRFASTHT DSSEQSVSLA
     DYIARMKEGQ KAVYYITADS YVAAKNSPHL ELFNKKGIEV LLLSDRIDEW MLSYLTEFDG
     KPLQSITKAD LDLGDLADKT EAEKEKAQDE ALSGFIERVK TLLGERVKDV RLTHRLTDTP
     AVVSTDNDQM TTQMAKLFAM SGQPVPEVKY TFELNPDHAL VKKTAALTDE SAFADWVELL
     LEQAMLSERG TLENPTAFIK RVNTLLAG