ID G6AEI3_9BACT Unreviewed; 853 AA.
AC G6AEI3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9138_00510 {ECO:0000313|EMBL:EHG17182.1};
OS Prevotella histicola F0411.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=857291 {ECO:0000313|EMBL:EHG17182.1, ECO:0000313|Proteomes:UP000004597};
RN [1] {ECO:0000313|EMBL:EHG17182.1, ECO:0000313|Proteomes:UP000004597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0411 {ECO:0000313|EMBL:EHG17182.1,
RC ECO:0000313|Proteomes:UP000004597};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Blanton J.M., Baranova O.V., Tanner A.C., Mathney J.M.J., Dewhirst F.E.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z.,
RA Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella histicola F0411.";
RL Submitted (OCT-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:EHG17182.1}.
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DR EMBL; AFXP01000003; EHG17182.1; -; Genomic_DNA.
DR RefSeq; WP_008822427.1; NZ_JH376762.1.
DR AlphaFoldDB; G6AEI3; -.
DR STRING; 857291.HMPREF9138_00510; -.
DR GeneID; 66731012; -.
DR PATRIC; fig|857291.3.peg.504; -.
DR HOGENOM; CLU_005070_4_1_10; -.
DR Proteomes; UP000004597; 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:SF193; CHAPERONE PROTEIN CLPB; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 1.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000004597};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 444..479
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 162..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 853 AA; 95702 MW; D50E49AB9DA012A0 CRC64;
MINQFSPKVS EILSFSKEEA ERLTSRSIAP EHIMLAILRE KSGPVWEIIN QKKIDIEYLK
KDIEKRIKEK SNISESVKGP DMLLNEHANN ILRLAVLEAR LQHAQTVDII HLFLAILHDS
SNNGAKQAFD VHGFSYNNVI SMFTASAKQP KNGIGMADEE EEIDDNMVSS PNSNTKTTSS
SRTRSKTPVL DSFGTDLTQA ATEGKLDPVV GREKEIMRVS EILGRRKKNN PILIGEPGVG
KSAIVEGLAQ LIVKHLTSPI LFDKRVIILD LTAVVAGTKY RGQFEERIRA LIKEIELNPD
VIIFIDEIHT LIGAGSSPGS MDAANILKPA LARGTIQCIG ATTLDEYRNS IEKDGALERR
FQKVQVEPTT TDETLQILEN IKDRYETHHH VSYTEDSLRA CVKYADRYIT DRFFPDKAID
IIDEVGSRMR LQHIKLPQSI LDIQKEIEIT QEKKQSAVKN QNFELAASFR DKQAELEQTL
KTEQEKWQKG DDTDKVEVNE GDIASVVSMM TGVPVQRMQE AESIRLKNMS NELKKLVVAQ
NPAIDKIVKA ILRNRVGLKD PNHPIGAFMF LGPTGVGKTY LAKQLAKIMF GSADALIRID
MSEYTESFNT SRLIGAPPGY VGYEEGGQLT EQVRRHPYSI VLLDEIEKAH GNVYNMLLQV
LDEGRLTDGN GRLIDFRNTV IIMTSNAGTR QLKEFGQGIG FKASTINGLS HGEQDKERAR
AIIQKSLSKQ FAPEFLNRLD EIITFDQLDL EAIKKIIDIE LKGLFKRVEE LGYTIKLTDE
AKEFVATKGY DVQFGARPLK RAIQNYIEDG LSELILSDKL TLGDTIYISK INDENSLNFT
IQNDSIRKVE PTN
//