ID A0Q272_CLONN Unreviewed; 765 AA.
AC A0Q272;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE SubName: Full=Negative regulator of genetic competence clpC/mecB {ECO:0000313|EMBL:ABK60429.1};
GN OrderedLocusNames=NT01CX_0220 {ECO:0000313|EMBL:ABK60429.1};
OS Clostridium novyi (strain NT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415 {ECO:0000313|EMBL:ABK60429.1, ECO:0000313|Proteomes:UP000008220};
RN [1] {ECO:0000313|EMBL:ABK60429.1, ECO:0000313|Proteomes:UP000008220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT {ECO:0000313|EMBL:ABK60429.1,
RC ECO:0000313|Proteomes:UP000008220};
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
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DR EMBL; CP000382; ABK60429.1; -; Genomic_DNA.
DR RefSeq; WP_011722712.1; NC_008593.1.
DR AlphaFoldDB; A0Q272; -.
DR STRING; 386415.NT01CX_0220; -.
DR KEGG; cno:NT01CX_0220; -.
DR PATRIC; fig|386415.7.peg.1758; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_9; -.
DR OMA; MDMNRLT; -.
DR Proteomes; UP000008220; 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; 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; IPR001270; ClpA/B.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF175; ATP-DEPENDENT CLP PROTEASE, ATP-BINDING SUBUNIT CLPC; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00871; CLPAB_2; 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:UP000008220}.
FT DOMAIN 174..320
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 504..676
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 675..764
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 380..407
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 765 AA; 86972 MW; A6A015CF1021EEDB CRC64;
MEMCSICKKN IATIYTAKIE DGKTKMVGIC LECAKKMGMP IMDQFMKQAG ITSEDMDNLT
EQMNKVFEET NIDDLANNNF LTNVLNGIFP KNDEEDYADN LDSLEFDKEK TSEKDKTNSE
GIRTKNIFKN KKKTKYLNKY GINLTDKAKE HKVDKVVGRN REIDRVIQIL NRRNKNNPIL
IGEPGVGKTA IAEGLAVRIS EKNVPAKLFE TEVYLLDLTA VVAGTQFRGQ FESRMKSIID
EAKSNGNVIL VIDELHNIMG AGEAQGGSMN AANILKPALA RGEIQVIGAT TLDEYRKYIE
KDSALERRFQ PVLVEEPTVE ETIEILEGIK DYYEQYHQVK ISHEVIENAV NLSERYINDR
FLPDKAIDVI DEASSRANLK NKGLVELKSL EDELEKVQNE KQKAADSDDY EKAAECKVEE
CRLKDKIDEL RKQCTDVELT TEDIAFVIEA WTKIPVQRIT EEEGEKLINL EERLHKRVIG
QNEAVKSLGR AIRRNRLGFR KKKKPASFIF VGPTGVGKTE LVKALASDLF ESEDALIRID
MSEYMEKHTV SKLIGAPPGY VGYDNGGQLT EKVRRKPYSV ILLDEIEKAH PDVFNMLLQI
LEDGRLTDSQ GRMVSFENTV IIMTSNVGTN FKSDSIGFGK EGYDAMEIRV KEALKETFRP
EFINRIDEIV VFNNLNKEEL YKIIDLMIDE VKNEIKGKKL TLTIDDTVKD YILKIGYDKK
YGARPLRRAI QRHIEDEIAE AYLLKKFKEG SNINAKVVDD KIVLE
//