ID H1FZU2_9GAMM Unreviewed; 628 AA.
AC H1FZU2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=ECTPHS_00220 {ECO:0000313|EMBL:EHQ51079.1};
OS Ectothiorhodospira sp. PHS-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ51079.1, ECO:0000313|Proteomes:UP000005314};
RN [1] {ECO:0000313|EMBL:EHQ51079.1, ECO:0000313|Proteomes:UP000005314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ51079.1,
RC ECO:0000313|Proteomes:UP000005314};
RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA Hoeft S., Oremland R.S., Stolz J.;
RT "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT oxidoreductases.";
RL Submitted (JAN-2012) 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:EHQ51079.1}.
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DR EMBL; AGBG01000001; EHQ51079.1; -; Genomic_DNA.
DR RefSeq; WP_008930646.1; NZ_AGBG01000001.1.
DR AlphaFoldDB; H1FZU2; -.
DR STRING; 519989.ECTPHS_00220; -.
DR PATRIC; fig|519989.5.peg.45; -.
DR eggNOG; COG0326; Bacteria.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000005314; 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};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:EHQ51079.1}.
FT DOMAIN 30..187
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 556..628
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 628 AA; 71431 MW; CD059CEFC9ADF220 CRC64;
MSVDTHKETR QFQTEVSQLL HLMINALYSN KEIFLRELIS NAADACDKLR FEALSDDALM
EGQRELQIQV SFDKEARTIT VRDNGIGMSR EEVIQNIGTI ARSGTREFIG KLTGDQKKDA
HLIGQFGVGF YSAFIVADRV TLTTRRAGMT PEHGVRWVSD GSGEFSVETV EKAERGTEVV
LHLKADEDEF LDQWRLRHII TRYSDHIPLP IAMPGTDDQG ESNGEWETVN RANALWTRPK
SEITDDEYKA FYKHVGHDFE DPLAWTHNRV EGRQEYTSLL YIPTRAPFDL WDRDRRHGIK
LYVQRVFIMD DAEHLMPTYL RFVRGVVDSS DLPLNISREI LQSNKLIDGM RSGSVKKVLG
LLEDMAANEP EKYQGFWDAF GRVMKEGPGE DYANREQIAR LLRFASTHTG ESAQTVSLAD
YVARMKEGQQ HIYYITADSH TAALHSPHLE VFRKRGIEVL LLSDRVDEWL VSHLHEFDGK
SLKSVAKGEL DLGDTETEEE KQAQQAAEEK VRDLLPRIKA ALEERVEDVR FSHRLTDSPA
CIVLSEHDMA LYMQQLLKQA GQNLPDTRPV LEVNPAHRLI ERMGEETDDA RFADWASLLM
DQAILAEGGQ LEDPAGFVRR LNALITSG
//
