ID A0A0S7Z8C6_9SPIR Unreviewed; 622 AA.
AC A0A0S7Z8C6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 08-NOV-2023, entry version 24.
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=AMS17_17615 {ECO:0000313|EMBL:KPJ83389.1};
OS Spirochaetes bacterium DG_61.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1704237 {ECO:0000313|EMBL:KPJ83389.1, ECO:0000313|Proteomes:UP000050987};
RN [1] {ECO:0000313|EMBL:KPJ83389.1, ECO:0000313|Proteomes:UP000050987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_61 {ECO:0000313|EMBL:KPJ83389.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ83389.1}.
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DR EMBL; LJNB01000325; KPJ83389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7Z8C6; -.
DR PATRIC; fig|1704237.3.peg.2647; -.
DR Proteomes; UP000050987; 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; 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 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.
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}; Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 24..180
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..338
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 548..622
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 622 AA; 71794 MW; CCEE5A7AE0A667F9 CRC64;
MSIHKFQAEV TQLLHLIIHS LYSHKEIFLR ELISNASDAL DKLKYLTLTD SAYRNLSFEP
RIDIRFDEQN KKILEVSDTG IGMNEEELIE NLGRIASSGT RTFLERMTGD ARKDANLIGQ
FGVGFYSAFM VSDKVEVISR KAGEEKAFKW ISDGKGDYEV KEADREHNGT SVICHLNEEG
QEYTSQWRIE SIVEKYSNHI PFPIFLHYEE TQDEGGEQKK GKEHKVKQIN AASAFWKRPK
AELKEEDYVE FYKTLTHDQE TPLLYLHTHA EGALQYSTLF YVPKKAPPDM FMVDYQPGVK
LYVKRVFITD DVRELMPTYL RFVRGIIDSE DLPLNVSREM LQKNRTIVNI RNASVKKILG
ELVSLKEKDS EKYELFYGQY RIPLKEGLYQ DFSNRDTLIE LVQFKSTKAD GYSSLSLYKD
RMKEDQKVIY YITGGNEENL RNSPLLEVYR ERDIEVLIMD DEIDEIVIPA VGQYKNVDFR
SVNRSDAADE FKKDGDNTRN KKLQPLLKRI KKVLEDRVKD VRISARLSDS PACIVADGSD
PTIQMQHIMK VLGQEHEGDF KPILEINPDH PIIVKMGQVQ ESALFEDIAW LLLEQAMLIE
GAPPKNASTF ARRLNNIMTR AL
//
