ID A0A0P7C521_9BACT Unreviewed; 604 AA.
AC A0A0P7C521;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Molecular chaperone Hsp90 {ECO:0000313|EMBL:KPM47123.1};
GN ORFNames=AFM12_14975 {ECO:0000313|EMBL:KPM47123.1};
OS Jiulongibacter sediminis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Jiulongibacter.
OX NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM47123.1, ECO:0000313|Proteomes:UP000050454};
RN [1] {ECO:0000313|EMBL:KPM47123.1, ECO:0000313|Proteomes:UP000050454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN14-9 {ECO:0000313|EMBL:KPM47123.1,
RC ECO:0000313|Proteomes:UP000050454};
RA Liu Y., Du J., Shao Z.;
RT "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL Submitted (JUL-2015) 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:KPM47123.1}.
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DR EMBL; LGTQ01000012; KPM47123.1; -; Genomic_DNA.
DR RefSeq; WP_055149688.1; NZ_LGTQ01000012.1.
DR AlphaFoldDB; A0A0P7C521; -.
DR STRING; 1605367.AFM12_14975; -.
DR PATRIC; fig|1605367.3.peg.413; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000050454; 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; 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.
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:UP000050454}.
SQ SEQUENCE 604 AA; 69319 MW; C0C26FCCD92D5814 CRC64;
MSTEKGTISI NTENIFPIIK KFLYSDNEIF LRELVSNAVD ATQKIKKLSA MGKYDGELGD
LKINVAVDKE AKTITISDKG LGMTADEVKK YINQIAFSGA KDFLDKYKDV DDKNPIIGQF
GLGFYSAYMV AKEVEIHTKS YQDEPAVKWT CDGTTEYALE DIEKAERGTD IILHIAEDSE
EFLEEAKIEQ ILTKYGKFLP VEIEFKENVI NNPTPIWVKS PSDLKDEDYL AFYKELYPMS
EDPLFWIHLN VDYPFNLTGV LYFPKIKQDF QLSREKIQLY SRQVFITDDV KDIVPEFLQL
LHGVIDSPDI PLNVSRSYLQ ADGNVRKINS HITKKVADKL SELFKEDRKA FEEKWDSIGL
FVKYGIISDE KFYDRAKDFI LFKNTEGEYF TPEDYKTKVE ALQKDKDENT VVLYTSHPEK
QDSYIKAAKK REYDVIVLDD VLDSHFINTL EQKLEKVTFK RVDGDSLDKL IDKGLNEESV
LSDKEKEKVE GLFKELAGNN VVEIKALSSD DAPVSIVLPE FMRRWTDMSR INGQSNMFGE
MPTMYNLVVN GNSPVIAKML KLRGEEKRQT YAKQLYDLAL LSQGMLSGGN LTDFVNRTFE
EMAE
//
