ID B5CLH9_9FIRM Unreviewed; 716 AA.
AC B5CLH9;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein {ECO:0000313|EMBL:EDY33831.1};
GN ORFNames=RUMLAC_00300 {ECO:0000313|EMBL:EDY33831.1};
OS [Ruminococcus] lactaris ATCC 29176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=471875 {ECO:0000313|EMBL:EDY33831.1, ECO:0000313|Proteomes:UP000003254};
RN [1] {ECO:0000313|EMBL:EDY33831.1, ECO:0000313|Proteomes:UP000003254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY33831.1,
RC ECO:0000313|Proteomes:UP000003254};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Ruminococcus lactaris ATCC 29176.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDY33831.1, ECO:0000313|Proteomes:UP000003254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY33831.1,
RC ECO:0000313|Proteomes:UP000003254};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2008) 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:EDY33831.1}.
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DR EMBL; ABOU02000014; EDY33831.1; -; Genomic_DNA.
DR AlphaFoldDB; B5CLH9; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_2_9; -.
DR Proteomes; UP000003254; 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; 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; 2.
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 Kinase {ECO:0000313|EMBL:EDY33831.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003254};
KW Transferase {ECO:0000313|EMBL:EDY33831.1}.
FT REGION 476..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 82556 MW; 82505C0BF45B38A5 CRC64;
MQKEYKRITD CEQIKKECSK MAVKKGTLSI DSENIFPIIK KWVYSDHDIF VRELVSNGCD
AITKLKKLDM MGEYELPEGY KPKIEVIVNP EEKTMKFIDN GLGMTAEEVE EYITQIAFSG
ATQFLEKYKD KTTEDDMIGH FGLGFYSAFM VADEVQIDTL SYKEGAKPVH WASEGGTEYE
MQEGSRTTVG SEITLYLNED SLEFANEYRA REVLERYCSF MPVEIFLSRA NAEPEYDTID
EADVLDTDTV VEHITEEPKE GEEGEPKQKA KIVRRPVSIS DIHPLWTKNP SECTKEEYIE
FYRKVFMDYK EPLFWIHLNM DYPFNLKGIL YFPKINTEYE SIEGKIKLYN NQVFIADNIK
EVIPEFLMVL KGVIDCPDLP LNVSRSALQN DGFVNKVADY ISKKVADKLN GMFKTDRENY
EKYWDDISPF IKFGCLKDEK FGEKMKDSML YKNLEHKYLT LEDIIKEAKG EAEVEEAAKE
EAAKNEESKA GNTEAEAKSE EAESTDADAE KEPEKTRIFY VTDEVQQSQY INMFKAQGQD
AIILTHNIDS AFITYLEQKH QEVQFLRIDA DVHDSLKDEV AEDEKEAFQK TAESLVEIFR
KELGNDKLEV KVEKLKDDKV ASMAVLSEEN RRMQEMMKMY GMSGMDPSMF GSQATLVLNA
NHPLVQFLVE HKRSKNVPVI CKQLYDLAML AHKPLSPEEM TAFVQRSNEI MMLLTK
//
