ID A0A1H3HYC6_9RHOB Unreviewed; 613 AA.
AC A0A1H3HYC6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05444486_101737 {ECO:0000313|EMBL:SDY20437.1};
OS Lentibacter algarum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Lentibacter.
OX NCBI_TaxID=576131 {ECO:0000313|EMBL:SDY20437.1, ECO:0000313|Proteomes:UP000199026};
RN [1] {ECO:0000313|EMBL:SDY20437.1, ECO:0000313|Proteomes:UP000199026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24677 {ECO:0000313|EMBL:SDY20437.1,
RC ECO:0000313|Proteomes:UP000199026};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNPR01000001; SDY20437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3HYC6; -.
DR STRING; 576131.SAMN05444486_101737; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000199026; 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:UP000199026};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00505}.
FT REGION 1..329
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 542..613
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 613 AA; 68605 MW; 9286EB4C3B5E8FC3 CRC64;
MTEQTHNFEA DTGKILNIVI NSLYSDRDIF LRELLSNASD AIHKRKLLGQ TQPDILNSAE
DEILVAVDDK KKTVEIIDTG IGLNADDLTE TLGTIARSGT SSFLDSIEEA SDSKNAAKSL
IGKFGVGFYS AFMVAEKVVV TTRKAGENGA NTWESDGKAG YTITAVSDEH PVGTSIKLFL
RKDAKEYADL HKLKGLIKKY SDHIIVPIFV QSKDVEKEQA NSAQALWTKS PSEVSEEEYS
EFYKASLGAF DEPYITLHNK TEGSIDFTNL LYIPKTAPFD LFEPERKTKI SLYINRVFIS
QDVDGVIPTW LRFVKGILDT TSLDLNVSRE MVQNSPVIKK ISKSVTKRIL SELKKKLKKD
EAGYDTFWEQ FGKVLKEGLY EDYEYRDKIA EITRAYSLKH QKLISLDAYL EEMADKQDKI
YYLTADTLKQ AKTSPHLEGF KAKDIDVLLM TDPIDAFWMS QMGAYKEKSF LSISRDKYDL
SELSEETPNE AANEAETNSL ALLIKDCLGD AVEDVKVTTS LVESPVRLVA GEGGLDFNLE
RILKAQNPEF EGSKKTLEVN AEHSLVRKIP DLSPELQKAL SRVLFEQARV LDGEMPSDPQ
QFSKDLIAIG TAL
//
