HTPG_COXBU
ID HTPG_COXBU Reviewed; 633 AA.
AC Q83EL0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=CBU_0309;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Nine Mile Crazy / RSA 514;
RX PubMed=17088354; DOI=10.1128/iai.00883-06;
RA Coleman S.A., Fischer E.R., Cockrell D.C., Voth D.E., Howe D., Mead D.J.,
RA Samuel J.E., Heinzen R.A.;
RT "Proteome and antigen profiling of Coxiella burnetii developmental forms.";
RL Infect. Immun. 75:290-298(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 -!- DEVELOPMENTAL STAGE: More than twofold more abundant in the large cell
CC variant (LCV) stage than in the small cell variant (SCV) stage (at
CC protein level). LCVs are more metabolically active than SCVs.
CC {ECO:0000269|PubMed:17088354}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO89866.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016828; AAO89866.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_819352.2; NC_002971.3.
DR RefSeq; WP_026051156.1; NZ_CDBG01000001.1.
DR AlphaFoldDB; Q83EL0; -.
DR SMR; Q83EL0; -.
DR STRING; 227377.CBU_0309; -.
DR PRIDE; Q83EL0; -.
DR EnsemblBacteria; AAO89866; AAO89866; CBU_0309.
DR GeneID; 1208191; -.
DR KEGG; cbu:CBU_0309; -.
DR PATRIC; fig|227377.7.peg.302; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..633
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000062984"
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; 72774 MW; BC71210DD4B52271 CRC64;
MSLQPQAETL SFEAEVKQLL HLVAHSLYSN KEIFLRELIS NSSDAADKLR YQALSDAALY
ENDADLKIWI DFDKDNRTIT IRDNGIGMSR EEVIENLGTI AKSGTRAFRE LLAEKKAEDS
QLIGQFGVGF YSAFIVADRV VVRTRRAGMK ADQGVEWEST GEGEYTLKNI DKPTRGTEVV
LHLKESEEEF LDPLRLRAII 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
