HTPG_CAMJJ
ID HTPG_CAMJJ Reviewed; 608 AA.
AC A1VYN0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-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};
GN OrderedLocusNames=CJJ81176_0546;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000538; EAQ73192.1; -; Genomic_DNA.
DR RefSeq; WP_002869314.1; NC_008787.1.
DR AlphaFoldDB; A1VYN0; -.
DR SMR; A1VYN0; -.
DR STRING; 354242.CJJ81176_0546; -.
DR PRIDE; A1VYN0; -.
DR EnsemblBacteria; EAQ73192; EAQ73192; CJJ81176_0546.
DR KEGG; cjj:CJJ81176_0546; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_7; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000000646; 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; Stress response.
FT CHAIN 1..608
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014908"
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; 69624 MW; 6F6CE04B2E48280F CRC64;
MQFQTEVNQL LQLMIHSLYS NKEIFLRELI SNASDALDKL NFLSVSDDKY KSLKFEPKIE
IKIDKDKKTL SISDNGIGMD KDDLINNLGT IAKSGTKSFL ENLSGDAKKD SQLIGQFGVG
FYSAFMVASK IEVLSKKALD DKAYLWSSDA NGYEIDDANK EEQGTSITLY LKDDEFANAY
KIESIIEKYS NHIQFPIFME KEEFTPAKEG EEEGKTELKI SQINKANALW RMQKSSLKAE
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
