ID G5F2K1_9ACTN Unreviewed; 863 AA.
AC G5F2K1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 13-SEP-2023, entry version 58.
DE RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1008_00595 {ECO:0000313|EMBL:EHF02950.1};
OS Olsenella sp. oral taxon 809 str. F0356.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=661087 {ECO:0000313|EMBL:EHF02950.1, ECO:0000313|Proteomes:UP000003446};
RN [1] {ECO:0000313|EMBL:EHF02950.1, ECO:0000313|Proteomes:UP000003446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0356 {ECO:0000313|EMBL:EHF02950.1,
RC ECO:0000313|Proteomes:UP000003446};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Olsenella sp. oral taxon 809 strain F0356.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EHF02950.1}.
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DR EMBL; ACVE01000002; EHF02950.1; -; Genomic_DNA.
DR RefSeq; WP_009278385.1; NZ_JH376563.1.
DR AlphaFoldDB; G5F2K1; -.
DR STRING; 661087.HMPREF1008_00595; -.
DR PATRIC; fig|661087.3.peg.596; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_11; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000003446; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS50151; UVR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003446};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 436..471
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 144..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..478
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 163..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 94799 MW; F9CC093D208F842D CRC64;
MFEKFTDKAR KVMSLAQDEA RNLGKMYVGT EHLLLALIKE GEGIAAQSLA KLEVTYDETL
LTIKEISSEE SEPVPGGHIP FTPRAKRVLE DAYRETMTRG QTYIATEHLL LGIVAEGDGR
AMTALSRMGI SGDAIRNAVG ELMEQTSEEN SRRLPQGVGA PFGQQQFGGS QPSQASGDAS
MLEQYGRNLT KLASNGKLDP VIGRDREVER VMQVLARRQK NNPLILGDPG VGKTAVVEGL
AQLIASGDVP DILRGKQVWT LDVASLVAGS KYRGEFEERL KKVIGEVMES KEDILFIDEM
HTIIGAGAAE GSIDAASILK PPLSRGEIQV IGATTAEEYR KHIEKDSALE RRFQPVSVGE
PSVEDTLAIL RGLQDRYEKH HHVRYTEEAL AAAVTLSNRY VQDRFLPDKA IDIIDEAGAR
TRVHKTSLPP ELAQVDEELA RVKDEKAQAA SAQEFEEAAR LRDREKELSA KRDELEAAWR
ERLDANVVVV DEADIADVVS EITGVPVSNL TEAEASKLLR AEEALHQRVV GQDEAVTKVS
KAIRRSRSPL KDPRRPGGSF IFLGPSGVGK TELAKSLAEF LFGSEDALIS FDMSEFMEKH
SVSKLVGAPP GYVGYDEGGE LTKAVRRRPY SVVLFDEIEK AHPDVFNILL QILDEGRLTD
GQGRTVDFSN TVIIMTSNIG AREIAQTAPM GFSAQGNGGL SDKEIRSRVE GELKRLFRPE
FLNRVDEIVV FKSLEAQQLR GIVELMVGEL RNRLIGQGMS IELTDAARDF VAKEGTDPVY
GARPLRRAIQ TLIEDRLAEE LLQGKWKAGD IVLVDSDGKE LSFSRGEGEI PSITERVHME
LPRARSHWSP TPHAPEGAVS SEG
//