ID A0A024FJJ9_9FLAO Unreviewed; 636 AA.
AC A0A024FJJ9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Chaperone protein HtpG {ECO:0000313|EMBL:BAO76723.1};
GN ORFNames=WPG_2493 {ECO:0000313|EMBL:BAO76723.1};
OS Winogradskyella sp. PG-2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=754409 {ECO:0000313|EMBL:BAO76723.1, ECO:0000313|Proteomes:UP000031636};
RN [1] {ECO:0000313|EMBL:BAO76723.1, ECO:0000313|Proteomes:UP000031636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-2 {ECO:0000313|EMBL:BAO76723.1,
RC ECO:0000313|Proteomes:UP000031636};
RX PubMed=24874677; DOI=10.1128/genomeA.00490-14;
RA Kumagai Y., Yoshizawa S., Oshima K., Hattori M., Iwasaki W., Kogure K.;
RT "Complete Genome Sequence of Winogradskyella sp. Strain PG-2, a
RT Proteorhodopsin-Containing Marine Flavobacterium.";
RL Genome Announc. 2:e00490-14(2014).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; AP014583; BAO76723.1; -; Genomic_DNA.
DR RefSeq; WP_045473020.1; NZ_AP014583.1.
DR AlphaFoldDB; A0A024FJJ9; -.
DR STRING; 754409.WPG_2493; -.
DR KEGG; win:WPG_2493; -.
DR HOGENOM; CLU_006684_3_2_10; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000031636; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
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 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; 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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031636}.
FT REGION 210..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 72538 MW; B2C6A979A4375704 CRC64;
MTKGSINVSV ENIFPLIKKF LYSDHEIFLR ELISNGTDAT LKLKHLTSIG ESKSEYGNPQ
LEIKIDKEGK KLHVIDQGLG MTADEVEKYI NQVAFSGAEE FLDQYKDSAK DSGIIGHFGL
GFYSAFMVAE KVEIITKSHT GAPAAHWTCD GSPEFTLVEA DKEDRGTEII LHIAEDSLEF
LEEARIRELL NKYNKFMPIP IKFGTKEVND PDFTPKTTKD KDGKETTEPH KQITVDDIIN
NPNPAWTKQP TELEDQNYKD FYRELYPMQF EEPLFNIHLN VDYPFNLTGI LYFPKMTNDL
NIQKDKIQLY QNQVFVTDNV EGIVPEFLTM LRGVIDSPDI PLNVSRSYLQ ADGNVKKISS
YITRKVADKL KSLFNNSRED FEAKWDDIKI VIEYGMLSEE KFFEKADAFA LYPTVDGKFY
TFEELTNAIK AKQTDKDDKM VILYASNKDE QHSYIESAKA KGYEVLMLDS PIVSHLIQKL
ETTKENISFA RVDGDHIDNL IKKDDTAISK LTDEEKTKLD DLLKAVVPSE KFSIQLEAMD
SNASPFIITQ PEFMRRMKEM QATGGGGMNM FGNMPEIHNL IVNTNSELVG EILNTKTKKK
QERLINQSLD LARLSQGLLK GEELTNFIKR SYDMIK
//
