HTPG_WOLSU
ID HTPG_WOLSU Reviewed; 618 AA.
AC Q7M8C4;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=WS1737;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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; BX571661; CAE10761.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7M8C4; -.
DR SMR; Q7M8C4; -.
DR STRING; 273121.WS1737; -.
DR PRIDE; Q7M8C4; -.
DR EnsemblBacteria; CAE10761; CAE10761; WS1737.
DR KEGG; wsu:WS1737; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_7; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000000422; 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; 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; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
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..618
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000063026"
FT REGION 1..331
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 332..541
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 542..618
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 618 AA; 71183 MW; 4F67DFA9322DD2EC CRC64;
MAKHTFQTEV NQLLDLMIHS LYSNKEIFLR ELISNASDAL EKLQYLTLTD ENLKNLQYTP
RIDIHFDEEK KILTLSDTGI GMNESDLVEN LGTIAKSGTK SFVSRLSGDK KKDSALIGQF
GVGFYAAFMV ADKIVVTTKK AGEESAYAWL SEGKGDYEIT PCSKESHGTE IKLFLKEEEK
EFASRWRLEE IIKKYSDHIP FPIFLHYTQK KNDQEESKEE QVNKAFALWR ISKNELKEED
YKEFYKSLSH DSHDPLAWVH IKVEGSQEYT TLFYLPSKAP FDLYRVDYRS GVKLYVKRVF
ITDDDKELLP SYLRFVRGII DSEDLPLNVS REILQQNRIL ANIKSASTKK ILAEIENLAK
DEEKYEAFFK EFGRALKEGL YGDFENKEKL LELMRFHSSL SPNKKISLQS YKERMKEGQK
AIYYLMGENA DLLQNSPLLE KFKKREIEVL FFDEEIDSIV MPMVNQYGDL PLKAINSAEA
DKDFEEESVS EEEKERFKPL LERFEKALSG EIKSVRLSKR LVDSPACVVA DEDDPNFAMI
KMMRQMGNAL GDFPEPKPIL ELNPEHPMVG KLLALEDEER ASDYAHLLLD QAKLLESGSL
KDAVGFAKRL NAMLERAI