ID A0A0M2NPV7_9FIRM Unreviewed; 633 AA.
AC A0A0M2NPV7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=CHK_0235 {ECO:0000313|EMBL:KKI52250.1};
OS Christensenella hongkongensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Christensenellaceae;
OC Christensenella.
OX NCBI_TaxID=270498 {ECO:0000313|EMBL:KKI52250.1, ECO:0000313|Proteomes:UP000034076};
RN [1] {ECO:0000313|EMBL:KKI52250.1, ECO:0000313|Proteomes:UP000034076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKU16 {ECO:0000313|EMBL:KKI52250.1,
RC ECO:0000313|Proteomes:UP000034076};
RA Lau S.K., Teng J.L., Huang Y., Curreem S.O., Tsui S.K., Woo P.C.;
RT "Draft genome sequence of bacteremic isolate Catabacter hongkongensis type
RT strain HKU16T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KKI52250.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAYJ01000030; KKI52250.1; -; Genomic_DNA.
DR RefSeq; WP_046442142.1; NZ_SMCZ01000011.1.
DR AlphaFoldDB; A0A0M2NPV7; -.
DR STRING; 270498.CHK_0235; -.
DR PATRIC; fig|270498.16.peg.1818; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000034076; 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; 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_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 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 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.
DR PROSITE; PS00298; HSP90; 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:UP000034076};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT REGION 1..349
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 561..633
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 633 AA; 72939 MW; 2ACF7E242E207A3E CRC64;
MAKKQFKAES KRLLDLMINS IYTHKEIFLR ELISNASDAI DKLVYRSLSD GGTGLNRSDF
YIRIEPDREK RILKITDNGI GMNREELESN LGVIARSGSL QFKNDMAEGE QQQEDIDIIG
QFGVGFYSAF MVSDKITVLS KKYGEEEGYK WQSSGADGYT ITPYEKDTQG TEIIMEIKSD
AEGEDYSRFL NENSLAALVK KYSDYVRYPV QMEMERSRNV NEGKEGAEPE WETYRELETL
NSMTPIWQRN KNEVKQKDLD NFYKEKFFDF ENPLKTIRVD AEGMINYKAL LFIPAKASYD
YFTKEYKKGL QLYSSGVMIM ERCEELVPEH FRFVRGIVDS PDISLNISRE MLQQTRQLRA
IASNLEKKIQ GELEKMLKND RESYETFWKA FGLQLKYGVM AEYGAHKDSL KNLLLFHSSA
GEKLTSLAEY AGRMKEGQKS IYYATGDSIR HIASLPQAEY IREKGYEILY FTDEADEFMA
QALMQYDDKP IKSINSADDD LKTEDEKKEI EKQGEENKEL LDFVKEALGD RIAKARISGK
LRSQPVCLTT EGPLSFEMEK YLAQVQPDSK MKAERVLELN AEHPVFQTLK ELEKTDREKA
KAYAQILYHQ AELMAGLPIE DPAAYSELVF SLM
//
