ID C3FX14_BACTU Unreviewed; 811 AA.
AC C3FX14;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Negative regulator of genetic competence {ECO:0000313|EMBL:EEM73740.1};
GN ORFNames=bthur0009_770 {ECO:0000313|EMBL:EEM73740.1};
OS Bacillus thuringiensis serovar andalousiensis BGSC 4AW1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527032 {ECO:0000313|EMBL:EEM73740.1};
RN [1] {ECO:0000313|EMBL:EEM73740.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4AW1 {ECO:0000313|EMBL:EEM73740.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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:EEM73740.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACNG01000006; EEM73740.1; -; Genomic_DNA.
DR RefSeq; WP_000971179.1; NZ_CM000754.1.
DR AlphaFoldDB; C3FX14; -.
DR GeneID; 83633702; -.
DR HOGENOM; CLU_005070_4_2_9; -.
DR Proteomes; UP000001380; Chromosome.
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; IPR028299; ClpA/B_CS2.
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; 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; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 418..453
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 414..471
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 811 AA; 90530 MW; A47E925EB712016C CRC64;
MMFGRFTERA QKVLALSQEE AIRIGHNNIG TEHILLGLVR EGEGIAAKAL IALGLSPEKV
QKEVEALIGR GTEASQTVHY TPRAKKVIEL SMDEARKLGH SYVGTEHILL GLIREGEGVA
ARVLNNLGVS LNKARQQVLQ LLGSNEASSG HQGGSSTNAN TPTLDSLARD LTVVARENRL
DPVIGRGKEI QRVIEVLSRR TKNNPVLIGE PGVGKTAIAE GLAQQIVNNE VPETLRDKRV
MTLDMGTVVA GTKYRGEFED RLKKVMDEIR QAGNIILFID ELHTLIGAGG AEGAIDASNI
LKPSLARGEL QCIGATTLDE YRKYIEKDAA LERRFQPIHV DEPSLDESTQ ILKGLRDRYE
AHHRVSITDD AIDAAVKLSD RYITDRFLPD KAIDLIDEAA SKVRLRSYTT PPNLKELEVK
LEEIRKEKDA AVQSQEFEKA ASLRDMEQRL REKLEDTKRQ WKEQQGKENS EVTVEDIANV
VSTWTRIPVS KLAQTETDKL LNLESILHDR VIGQDEAVVA VAKAVRRARA GLKDPKRPIG
SFIFLGPTGV GKTELARALA ESMFGDEDAM IRIDMSEYME KHSTSRLVGS PPGYVGYEEG
GQLTEKVRRK PYSVVLLDEV EKAHPDVFNI LLQVLEDGRL TDSKGRTVDF RNTIVIMTSN
VGAEALKRNK HLGFNVQDES RDYSDMKGKV MDELKKAFRP EFLNRIDEII VFHMLEKKHI
QEIVTLMVNQ LVNRLKEQEI ELHLTEGAIS AIADKGFDRE YGARPLRRAI QKHVEDRLSE
ELLKGAIEKG QKVIFDVEGE SFVIHSAEKV K
//
