ID B1IGI4_CLOBK Unreviewed; 811 AA.
AC B1IGI4;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Putative negative regulator of genetic competence MecB/ClpC {ECO:0000313|EMBL:ACA46868.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:ACA46868.1};
GN OrderedLocusNames=CLD_0992 {ECO:0000313|EMBL:ACA46868.1};
OS Clostridium botulinum (strain Okra / Type B1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498213 {ECO:0000313|EMBL:ACA46868.1, ECO:0000313|Proteomes:UP000008541};
RN [1] {ECO:0000313|EMBL:ACA46868.1, ECO:0000313|Proteomes:UP000008541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okra / Type B1 {ECO:0000313|Proteomes:UP000008541};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP000939; ACA46868.1; -; Genomic_DNA.
DR RefSeq; WP_003404310.1; NC_010516.1.
DR AlphaFoldDB; B1IGI4; -.
DR KEGG; cbb:CLD_0992; -.
DR HOGENOM; CLU_005070_4_1_9; -.
DR Proteomes; UP000008541; 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 Hydrolase {ECO:0000313|EMBL:ACA46868.1};
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..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 419..454
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 141..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 415..465
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 141..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 91971 MW; A7DC84C6B17A0691 CRC64;
MMFGRFTERA QKVLMNAQEE AEKFKHGYVG TEHILLGILI EDGVAKELLN NFSITEDKVR
QLIERYEGKG EMDLYKNEIP LTPRTKRLLE MSLLEARNLN HNYITPEHIL LGLIREAEGV
AFTILSNLGL DAERLRKELI KNLSGQETPK DEGSKKSSKS STPTLDQFGR DLTEMAEEGK
VDPVIGRDKE TQRVLEILCR RTKNNPCLIG EPGVGKTAIA EGLAQNIIDG NIPEILKNKR
VVTLDLTSMI AGAKYRGEFE DRLKKIMEEV RSSKDTILFI DEIHTIVGAG AAEGAIDAAN
ILKPALARGE IQCIGATTLD EYRKYIEKDS ALERRFQPIN VGEPTKEETI EILKGLRDKY
EAHHRVKFTD DAIYAAVNLS DRYIRDRFLP DKAIDLMDEA GSKVRIQNLI APPDLKNIEE
QLDKVVKEKE DAIRVQDFEK AANLRDKEKE LKEKLEGLKK DWNAEKEGSN LIVSEQQIAA
VVSNWTNIPV NKLTEKESER LLKLEDILHN RVIGQEEAIK SVSRSVRRAR VGLKDPKRPI
GSFIFLGPTG VGKTELTKAL AEAMFGNENN MIRVDMSEYM EKHSVSRLIG SPPGYVGHDE
GGQLTDKVRT NPYSVVLFDE IEKAHPEVFN ILLQILEDGR LTDGKGKTVD FRNTIIIMTS
NVGASTISRQ KTLGFNTSIE EERETEYEKM KDNIMNELKH SFRPEFLNRI DDIIVFHQLR
EEHIREIVKL MLKTVSNRVK DQGIKLEFTE EAEKILAKEG YDTNYGARPL RRAITKIVED
KLSEEILKGN IKKGDSVKVN TIEDKLNFCK M
//
