ID A0A257SWT3_9GAMM Unreviewed; 626 AA.
AC A0A257SWT3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=B7Z66_04240 {ECO:0000313|EMBL:OYV77604.1};
OS Chromatiales bacterium 21-64-14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales.
OX NCBI_TaxID=1970504 {ECO:0000313|EMBL:OYV77604.1, ECO:0000313|Proteomes:UP000215939};
RN [1] {ECO:0000313|EMBL:OYV77604.1, ECO:0000313|Proteomes:UP000215939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21-64-14 {ECO:0000313|EMBL:OYV77604.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYV77604.1}.
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DR EMBL; NCBI01000004; OYV77604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257SWT3; -.
DR Proteomes; UP000215939; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 30..187
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..333
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 551..626
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 492..519
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 626 AA; 71627 MW; 1A2303850354EB98 CRC64;
MSVEAHKETL SFQAEVRQLL NLMIHSLYSN KEIFLRELIS NAADACDKLR FEALTDDALY
EGDSDLAVCI SVDRERRTVT VADNGVGMTR AEVMDNIGTI ARSGTRQFLN SLTGDQSKDT
QLIGQFGVGF YSAFIVADRI TLVTRRAGLG PEHGVRWESD GQGDYSLETM ERPGRGTEVT
LHLREGEDEF LEGLRLRTIV RKYSDHVPLP VRMRKEGDAG LETLNRASAL WGRRRNEITD
EEYKEFYKHV AHDFEDPLVW VHNHVEGKVS YHSLLYIPAR PPFDLWDRER RHGLKLYVRR
VFIMDDTEHL LPQYLRFVRG VVDSEDLPLN VSREILQHNR EIEQIRSALV KRLLTTLEEM
SANEPEQYAR FWESFGKVMK EGPAEDYANR DQIAGLLRFS STHADRPVQD VSLKDYLARM
KPGQDKIYYL TAESFAAARN SPHLERLRKK DVEVLLLCDR VDEWLVSHLT EFDGKPLHSV
AKGDLELGAL EDQEEKRSVE QAESDYKELL ERMSAALGER VKEVRVTHRL TTSPACLVLD
EHDMPVHLQR MLKAAGQEVP SAHPILEINP GHLLVQRLKD EQDPQRFSDW ASILFDQALL
ADGGQLEDPA AFVGRLNELL LLLTRK
//
