ID R6BD73_9CLOT Unreviewed; 632 AA.
AC R6BD73;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein {ECO:0000313|EMBL:CDA61180.1};
GN ORFNames=BN513_00991 {ECO:0000313|EMBL:CDA61180.1};
OS Clostridium sp. CAG:169.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262778 {ECO:0000313|EMBL:CDA61180.1, ECO:0000313|Proteomes:UP000018302};
RN [1] {ECO:0000313|EMBL:CDA61180.1, ECO:0000313|Proteomes:UP000018302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:169 {ECO:0000313|Proteomes:UP000018302};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDA61180.1}.
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DR EMBL; CBCF010000041; CDA61180.1; -; Genomic_DNA.
DR AlphaFoldDB; R6BD73; -.
DR STRING; 1262778.BN513_00991; -.
DR Proteomes; UP000018302; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:CDA61180.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018302};
KW Transferase {ECO:0000313|EMBL:CDA61180.1}.
SQ SEQUENCE 632 AA; 73328 MW; BF7A57CCA00D6EDA CRC64;
MKREGQISVN SKNMFPIIKK WLYSDKDIFL REIVSNSCDA IKKLISLRGI GQAPQEDGYQ
PRVEVRIDSE KKQLIVSDNG IGMTEDEVER YITQVAFSGA EEFLQKYGED ASEAAGIIGH
FGLGFYSSFM VSDTVEIQTL SFQPDAKPVH WTSSGEDSYE IEDGERTEHG TTIIMNITEG
EEEFLQESRI REILNKYCQF MPYEIYLNPH DEQRPVYDKD GNVEKNEDGT DKMRTVKPLP
VNDTQPLWLK SPSECTDEEY KAFYQKVFMD FNEPLFWIHL NVDYPFNLKG ILYFPKQVNR
LEVVPGQVKL YSNQVFVADN IKEVIPEFLL LLKGVIDCPD MPLNVSRSFL QNDGQVQKIA
QHITKKVSDK LHQIFKNDRE TYEKYWNDIS AFIKFGCLKD EKFYDRMKDI LLLHTIDGEY
KTLEEYPKAD ENKIYYVTDE NLQAQYISMF RQNGLTAAVL THVIDPHFIS MLEYKEQEKL
KFLRIDSDLG SALKTEQTEE EKQQQEEQDK QLIERFKQAL PEEKLEYQVE SLKSDETPAV
ILLSEYARRI QDMSRAFGES FGGPAQVTLV LNRENPIIRS LETLPDDKRE LVCKQVYDLA
QLAHKPLSAE QMQGFMRRSM QLLGMVTGES HQ
//