ID A0A167K9X9_9FLAO Unreviewed; 629 AA.
AC A0A167K9X9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:OAB81546.1};
GN ORFNames=ULVI_01630 {ECO:0000313|EMBL:OAB81546.1};
OS Cochleicola gelatinilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cochleicola.
OX NCBI_TaxID=1763537 {ECO:0000313|EMBL:OAB81546.1, ECO:0000313|Proteomes:UP000077013};
RN [1] {ECO:0000313|EMBL:OAB81546.1, ECO:0000313|Proteomes:UP000077013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0005 {ECO:0000313|EMBL:OAB81546.1,
RC ECO:0000313|Proteomes:UP000077013};
RA Shin S.-K., Yi H.;
RT "Ulvibacter sp. LPB0005, isolated from Thais luteostoma.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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:OAB81546.1}.
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DR EMBL; LRXL01000012; OAB81546.1; -; Genomic_DNA.
DR RefSeq; WP_068588910.1; NZ_LRXL01000012.1.
DR AlphaFoldDB; A0A167K9X9; -.
DR STRING; 1763537.ULVI_01630; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000077013; Unassembled WGS sequence.
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; 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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077013}.
FT REGION 207..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 71910 MW; EA48D5A9E4BE1E55 CRC64;
MSQGTINVSV ENIFPLIKKF LYSDHEIFLR ELISNATDAT LKLKHLTSIG EAKVTYGNPV
IEVKIDKENK QLHIIDQGIG MTKEEVEKYI NQIAFSGAEE FIEKYKDKQG DETGIIGHFG
LGFYSAFMVA NKVEIITKSY KDEPAAHWTC DGSPNYTLEE ADKKERGTEI ILHISEDETE
FLEEGKISGL LSKYNKFMPI PIKFGTRTET LPKPQDAKED DEAPTQEVDN IINNPNPAWT
KQPADLEDKD YKSFYRELYP SQFEEPLFNI HLNVDYPFNL TGILYFPKLT NDMSVQKDRI
QLYQNQVFVT DNVEGIVPEF LTMLRGVIDS PDIPLNVSRS YLQADGAVKK ISSYITRKVA
DKLKSLFNEN RKDFEAKWND IKIVIEYGML SEDKFFDKSK DFALYPTVDG SFFTFEELKD
KIKDAQTDKD DNLVILYASD KEAQHSYIET AKDKGYEVLL LDSPIVSHLI QKLEGANEKT
QFVRVDGDHI DNLIKKEDAS ISKLSEEEKE TLKTFLTETI PSEKFTVQLE AMDSSANPFI
ITEPEFMRRM KEMQQSGGGG MFGMGNMPEM YNLVVNTNNE LVTEILNTKT KKKKERLVTQ
ALDLAKLSKN LLKGEDLTAF IKRSYEMIK
//
