HTPG_CAMJ8
ID HTPG_CAMJ8 Reviewed; 608 AA.
AC A8FKU4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=C8J_0482;
OS Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS 11828).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=407148;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81116 / NCTC 11828;
RX PubMed=17873037; DOI=10.1128/jb.01404-07;
RA Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA van Vliet A.H.M.;
RT "The complete genome sequence of Campylobacter jejuni strain 81116
RT (NCTC11828).";
RL J. Bacteriol. 189:8402-8403(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; CP000814; ABV52081.1; -; Genomic_DNA.
DR RefSeq; WP_002866408.1; NC_009839.1.
DR AlphaFoldDB; A8FKU4; -.
DR SMR; A8FKU4; -.
DR KEGG; cju:C8J_0482; -.
DR HOGENOM; CLU_006684_3_0_7; -.
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..608
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000072455"
FT REGION 1..332
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 333..536
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 537..608
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 608 AA; 69681 MW; 547F52265ABD5472 CRC64;
MQFQTEVNQL LQLMIHSLYS NKEIFLRELI SNASDALDKL NFLSVSDDKY KSLKFEPKIE
IKIDKDKKTL SISDNGIGMD KDDLINNLGT IAKSGTKSFL ENLSGDAKKD SQLIGQFGVG
FYSAFMVASK IEVLSKKALD DKAYLWSSDA NGYEINDANK EEQGTSITLY LKDDEFANTY
KIESIIEKYS NHIQFPIFME KEEFTPAKEG EEEGKTELKI SQINKANALW RMQKSSLKVE
DYERFYEQNF HDSNKPLLYL HTKSEGKLEY NSLFFIPQNA PFDLFRVDYQ SGLKLYVKRV
FISDDDKELL PTYLRFVRGI IDVEDLPLNV SREILQENQI LKGVKEASVK KILGELEKLK
NNDKEKYLSF FKTFGKVLKE GLYGFGGEKD SLLKLMLYKS TKGENLRSLE EYKNDLQGEQ
KEIFYIAGNN ESLLRTSPLL EEYKQKNIEV LLMDDEIDSL VTPMLEFEGL KFVAINQVED
KNELSDEEKN TFAPLVAKFK ELLKDQVEDV RLTSRLKDSP SCIVYDKNKP DFAMQQLLKQ
MGQEQNFKPI LEINPKHAIF TGLKNNESFS ADIATLVLNM AKLSEGMGVD NPAEFNASLT
KIINKAFS