ID K6TV03_9CLOT Unreviewed; 644 AA.
AC K6TV03;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Molecular chaperone of HSP90 family {ECO:0000313|EMBL:EKQ51246.1};
GN ORFNames=A370_04991 {ECO:0000313|EMBL:EKQ51246.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ51246.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ51246.1, ECO:0000313|Proteomes:UP000001325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX PubMed=23405323;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA Midgley D.J., Hendry P.;
RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT Seam Gas Formation Water.";
RL Genome Announc. 1:E00081-12(2013).
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:EKQ51246.1}.
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DR EMBL; ALXI01000162; EKQ51246.1; -; Genomic_DNA.
DR AlphaFoldDB; K6TV03; -.
DR STRING; 1196322.A370_04991; -.
DR PATRIC; fig|1196322.3.peg.4852; -.
DR eggNOG; COG0326; Bacteria.
DR Proteomes; UP000001325; 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:UP000001325}.
FT REGION 214..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 74743 MW; 6B86D6BBA2F315BB CRC64;
MIKENGNISI DTENIFPIIK KWLYSDKDIF IREVISNACD AISKFQRLVS LGEASISGDE
QYKVVVSINK EKKTLKFIDN GIGMTEEEVK KYINQVAFSG ATDFMEKYKD KMDEGKDIIG
HFGLGFYSTF MVSTKVEIDT LSFKEGAEAV KWECTGGTEY EIGPTNERTT RGTTVTLFID
DESSEFLEEY KVREIIKKYC SFLPTEIYLE DENKPKEEPK YETKKKEDGT EYQELVEPEA
PKPLNDTNPL WVKAPKDCTD EEYKDFYRKV FMDFNEPLFW IHLNVDYPFN LKGILYFPKL
THEFEATEGQ VKLYNNQVFV ADNIKEVIPE FLLLLKGTID CPDLPLNVSR SFLQNDKEVS
KISNHIVKKV ADKLVDLFKN SREEFNKFWP DIQIFIKYGC LRDPKFYDKI KEIIIFKNLK
GEFVTLKDYL EANKEKHENK VFYANDEKQQ SQYIKMFKEY DLDAVILDCS LDDHFISFLE
MHESGVKFNR IDSDISDTLG SKADENDETV KALNKEIEDL FKNSLGDKIK NLTIEGLKNE
DTPALILVSE ESRRMAQMSK MYAKSGMNFP GMFDEEKTLV VNNKNVIIKK LIEISKNEAK
KEDVKFICEH ILDLAKIANK ELDANEMDEF IKRNNMLLNK VVAL
//
