ID G5F559_9ACTN Unreviewed; 661 AA.
AC G5F559;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 08-NOV-2023, entry version 59.
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=HMPREF1008_01124 {ECO:0000313|EMBL:EHF01500.1};
OS Olsenella sp. oral taxon 809 str. F0356.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=661087 {ECO:0000313|EMBL:EHF01500.1, ECO:0000313|Proteomes:UP000003446};
RN [1] {ECO:0000313|EMBL:EHF01500.1, ECO:0000313|Proteomes:UP000003446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0356 {ECO:0000313|EMBL:EHF01500.1,
RC ECO:0000313|Proteomes:UP000003446};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Olsenella sp. oral taxon 809 strain F0356.";
RL Submitted (AUG-2011) 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:EHF01500.1}.
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; ACVE01000009; EHF01500.1; -; Genomic_DNA.
DR RefSeq; WP_009278914.1; NZ_JH376563.1.
DR AlphaFoldDB; G5F559; -.
DR STRING; 661087.HMPREF1008_01124; -.
DR PATRIC; fig|661087.3.peg.1122; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_11; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000003446; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003446};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 22..183
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..359
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 587..661
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 661 AA; 73858 MW; 53B52E03AB865347 CRC64;
MKQFKTESKK LLDLMINSIY TNREIFLREL ISNASDAIDK LSFKSLTDPS VKLDADSLAI
RLSFDKDART ITVSDNGIGM TQEELDRNLG TIAHSGSEQF KEENAAHQGD EIDIIGQFGV
GFYSAFMVAD RVRVVSRAFG SDQAYAWESD GVKGYSIEPA AEGERSGEDD HGTDVTLYLR
EADSDDPEAG ESPDRFLSEW GLRDLVSRYS NYVRHPVQMM VSKSRELPRP EDAGDDYKPQ
YEEYQELETI NSITPIWKKR SSEVEQKDYD EFYRSAFHDW VDPARTISFH AEGSLSYDAL
LFIPGQAPFD LYSKDYEKGL ALYSSNVLIQ EKCADLLPDH YNFVRGVVDS PDVTLNISRE
TLQQNSQLRA IARRVEKKVT SELKGMLRDD REAYEKFFDN FGRGLKFGIY NSYGSKASEL
ADLLLFWSAR EGKMLTFAEY AEGMAEGQDK VYYAAGDSRE RLQKSPVVKS AVDHGFDVLL
CTQDVDEFMF QAMRSWHQDA VAGDSEHKGT DARDLELVNV STADLDLATE DEKKAAEEAT
SEHKGLFDEL KDALGEKVTG VRAAAGLGEA PATIAAEGPV SLEMERVIAR GPEGEMAPKA
QRVLQLNAAH PVFGKLVAAE EAGDKDRLKL YGDILYDQAL LVEGLPIDDP VQFAKNVTEL
M
//
