GenomeNet

Database: UniProt
Entry: A0A3M0BVU2_9PROT
LinkDB: A0A3M0BVU2_9PROT
Original site: A0A3M0BVU2_9PROT 
ID   A0A3M0BVU2_9PROT        Unreviewed;       651 AA.
AC   A0A3M0BVU2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=BXY39_3695 {ECO:0000313|EMBL:RMB01508.1};
OS   Eilatimonas milleporae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC   Kordiimonadaceae; Eilatimonas.
OX   NCBI_TaxID=911205 {ECO:0000313|EMBL:RMB01508.1, ECO:0000313|Proteomes:UP000271227};
RN   [1] {ECO:0000313|EMBL:RMB01508.1, ECO:0000313|Proteomes:UP000271227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25217 {ECO:0000313|EMBL:RMB01508.1,
RC   ECO:0000313|Proteomes:UP000271227};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) 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:RMB01508.1}.
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; REFR01000016; RMB01508.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0BVU2; -.
DR   InParanoid; A0A3M0BVU2; -.
DR   Proteomes; UP000271227; 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; 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.
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:UP000271227};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00505}.
FT   DOMAIN          44..199
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          1..357
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..651
FT                   /note="C"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   651 AA;  71859 MW;  912494B5A71BE889 CRC64;
     MADQSMADTT KENTADTKAK AEQHGFEAEV ARLLHLMVHS VYSEREIFLR ELISNASDAC
     DKLRYEALTK PDLTKDDPEF HIEIVADAKA KTLVIRDNGV GMNKDDLKAN LGTIARSGTA
     GFMDRLTGDA KRDVQLIGQF GVGFYSVFMV ADKVSVLTCR AGEDAAYLWE SDGSGTYSIA
     DGDKAGRGTE ITLHMKDDAG EFLERFRLER IVKTYSDHIA VPIRLAVSGA DEQEKTASGD
     EEKDDAPVNQ GSALWTRAKA DITDDQYTEF YRHVSHAFDE PAFRLHYTAE GMQQYSVLLF
     IPETRPMDLF DPARKSRVKL YVKRVFITDD TSGMLPGWLR FLRGVVDSQD LPLNISREML
     QNNPVLKRMS SAITKKVLGE LEKLAAKDAE KFEAIWSTFG AVIKEGLYED LERREALLKL
     VRFRTTDGDG WVSLADYVGR MKDKQSAIYY VTGPDEAAVK RSPQLEGFKA KGVEVLLLSD
     PVDDFWLQMV SDYEGKPFKS ITRGASDLSD IADGVAKDDK DKAPEGELTV LATLMKDVLG
     DAVSDVRASD RLTETAACLV ADDSAMDMHL ERMLKANNQI DMATPKILEI NPSHGLIKKL
     AALSGDKGAR DACDDAVHLL LDQAKILEGD PLDDPSAFAG RLAKAVENGL A
//
DBGET integrated database retrieval system