HTPG_COXBR
ID HTPG_COXBR Reviewed; 633 AA.
AC A9NB44;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=COXBURSA331_A0416;
OS Coxiella burnetii (strain RSA 331 / Henzerling II).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=360115;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 331 / Henzerling II;
RA Seshadri R., Samuel J.E.;
RT "Genome sequencing of phylogenetically and phenotypically diverse Coxiella
RT burnetii isolates.";
RL Submitted (NOV-2007) 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; CP000890; ABX78007.1; -; Genomic_DNA.
DR RefSeq; WP_012220162.1; NC_010117.1.
DR AlphaFoldDB; A9NB44; -.
DR SMR; A9NB44; -.
DR KEGG; cbs:COXBURSA331_A0416; -.
DR HOGENOM; CLU_006684_3_0_6; -.
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..633
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000081514"
FT REGION 1..344
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 345..560
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 561..633
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 633 AA; 72764 MW; 13BFF17EE699ADBF CRC64;
MSLQPQAETL SFEAEVKQLL HLVAHSLYSN KEIFLRELIS NSSDAADKLR YQALSDAALY
ENDADLKIWI DFDKDNRTIT IRDNGIGMSR EEVIENLGTI AKSGTRAFRE LLAEKKAEDS
QLIGQFGVGF YSAFIVADRV VVRTRRAGMK ADQGVEWEST GEGEYTLKNI DKPTRGTEVV
LHLKESEEEF LDSLRLRAII TKYSDHILLP IVMKKIKTSG ADDEDKNETP EEEVVNRANA
LWVLPKDKIK DEEYKELYKH IAHDFEDPLA WVHNKVEGKL EYTTLLYIPA RAPFDLWNRE
GQRGLKLYVK RIFIMDDAEH FMPMYLRFVK GIVDSNDLPL NISRELLQSN EVINKIKAGC
VKRILSLLED LAKNDKEKYA SFWKAFGQVL KEGPAEDFAN RDRIANLLRF ASTHNDTDEQ
NVSLQDYISR MKPEQNKIYY IVADTYTSAK NSPLLEVFRK KDIEVLLMSD RVDEWLVAHL
NEFEGKSLQS IAKGTLDLGD LEKEEKVETE KFEKDFDELL KQFKEVLGEK IKDVRITHRL
TDSPTCVVFD ENEMSGHLQR LLIQTGQDFM QAKPILEINP SHPLILRVKN ESDKTRFNRW
ADLLLNQALL AEGEQLKDPA SFVKGLNELL LDS
