HTPG_NITHX
ID HTPG_NITHX Reviewed; 638 AA.
AC Q1QHD7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Nham_3632;
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Nitrobacter.
OX NCBI_TaxID=323097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-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; CP000319; ABE64360.1; -; Genomic_DNA.
DR RefSeq; WP_011512001.1; NC_007964.1.
DR AlphaFoldDB; Q1QHD7; -.
DR SMR; Q1QHD7; -.
DR STRING; 323097.Nham_3632; -.
DR EnsemblBacteria; ABE64360; ABE64360; Nham_3632.
DR KEGG; nha:Nham_3632; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_5; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000001953; 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; 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; Reference proteome;
KW Stress response.
FT CHAIN 1..638
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000258516"
FT REGION 1..343
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 344..557
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 558..638
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 638 AA; 69605 MW; A073C02C60682C9A CRC64;
MTSTIDSDGA AESRVFEADV AKLLQMMVHS VYSDKDVFLR ELISNAADAC ERLRYDAISD
PALLADDARP QIAITIDAER RQLTVDDNGI GMSRDEMVDA LGTIARSGTK AFIEQAKVEQ
AKSAEAGDGV TVIGQFGVGF YSAFMVADQV DVISRRAGAG EAWRWSSDGK GTFTVTPADE
SEAPARGTRV MLHLTEDAKG YTDRLKLEQI VREQSGHVPV PIVLVEQPGA APTEIADGAA
LWTKPRGEIG TSEYVDFYRS VAGHFDEPAL TVHFRAEGRQ EFTALLFVPQ TRSFDLFETD
RKGPIKLYVK RVFITDDADL LPRYLRFVRG VVDSADLPLN ISREMIQESP ILAAIKKSIT
GRVLSELEKL AEKDAQAYGK VWEAFGPMFK EGIYDAADRR DAILSLCRFR TTAGSLRSLK
DYVGALKDNQ TSIYYLAGQD AARLEASPHL EGFRARGVEV LLLSDPVDSF WVTSAPSFEG
KPFKSVTQGD TDLAAIPRVD ASAETLQEVS ASVTEFLAFL KTTLADLVSD VRSSERLTDS
PVCLIAAESG PDRQLEKILV GVGQLTGASK PVLEVNPRHP LIASLAALGD GDRAFKEDTA
RMLLDDARVL DGDRPSDALE FSRRLARIVE RGLRGSTA