ID B4CV89_9BACT Unreviewed; 610 AA.
AC B4CV89;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Chaperone protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000256|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000256|HAMAP-Rule:MF_00505};
GN ORFNames=CfE428DRAFT_0027 {ECO:0000313|EMBL:EDY21902.1};
OS Chthoniobacter flavus Ellin428.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC Chthoniobacteraceae; Chthoniobacter.
OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY21902.1, ECO:0000313|Proteomes:UP000005824};
RN [1] {ECO:0000313|EMBL:EDY21902.1, ECO:0000313|Proteomes:UP000005824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY21902.1,
RC ECO:0000313|Proteomes:UP000005824};
RX PubMed=21460085; DOI=10.1128/JB.00295-11;
RA Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A.,
RA Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S.,
RA Larimer F.W., Land M.L., Hauser L., Sangwan P., de Vos W.M., Janssen P.H.,
RA Smidt H.;
RT "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic
RT heterotrophic soil bacterium.";
RL J. Bacteriol. 193:2902-2903(2011).
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000256|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505}.
CC Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239, ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDY21902.1}.
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DR EMBL; ABVL01000001; EDY21902.1; -; Genomic_DNA.
DR RefSeq; WP_006977354.1; NZ_ABVL01000001.1.
DR AlphaFoldDB; B4CV89; -.
DR STRING; 497964.CfE428DRAFT_0027; -.
DR GeneID; 78184766; -.
DR eggNOG; COG0326; Bacteria.
DR InParanoid; B4CV89; -.
DR Proteomes; UP000005824; Unassembled WGS sequence.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF44; HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00505};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00505};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00505}; Reference proteome {ECO:0000313|Proteomes:UP000005824};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:EDY21902.1}.
FT DOMAIN 26..182
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..320
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 531..610
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 610 AA; 68902 MW; 39B4F9F3DEB20E0A CRC64;
MSTTEKHAFQ AEIAQLLDLV IHSLYTDKEI FVRELISNAA DASEKLKFLQ TSGTEVFEPE
LPLKISVSTD GQAKTITFTD TGIGMTHGEL IDNLGTIAHS GSKAFLEQLK ANKDDANLIG
QFGVGFYSAF MVAEKVTVYT RSYQPGESGW VWSSDGRTGY EIDAASDLSR GTKIVVQLKD
TEFAQASNIE RIIKHYSNFV PFPIELNGNA VNTVQALWTK NKSEITDEEY NDFYKYVAHE
SEPPLYRLHF SADAPLSIRA LLFVPEKSYE LLTLARGENE VNLYCRKVLI QPKAKNLFPE
WLRFLKGVVD SEDLPLNISR ETMQDSALLR KINDVLTKRV LKWLDEEAKA DPEKFDKFFR
EHGHCLKEGV ANDYQHRETL AKLLRNESSH TDVGKTTSLT DYVGRMPEEQ KEIYYLTAPN
REAALASPYY EVFREKKFEV LFLYAPQDEI VMEQLREFDK KRLVAAEKAD LKLDKESSGA
LSEEDARVLA NFIKERLGDR VNEVHSSKRL VGSPAVVVDS DTHMTSSMRR MMKMMSREGE
APLESKPNLE INPDHAMLVR LNAIRQSDPA LAGEVAEQIF DNALVAAGLL EDPRAMLGRL
NGLLEKLLNK
//
