ID Q899V4_CLOTE Unreviewed; 767 AA.
AC Q899V4;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE SubName: Full=Negative regulator of genetic competence mecB {ECO:0000313|EMBL:AAO34716.1};
GN Name=mecB {ECO:0000313|EMBL:AAO34716.1};
GN OrderedLocusNames=CTC_00060 {ECO:0000313|EMBL:AAO34716.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO34716.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO34716.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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DR EMBL; AE015927; AAO34716.1; -; Genomic_DNA.
DR RefSeq; WP_011098389.1; NC_004557.1.
DR AlphaFoldDB; Q899V4; -.
DR STRING; 212717.CTC_00060; -.
DR GeneID; 24253228; -.
DR KEGG; ctc:CTC_00060; -.
DR HOGENOM; CLU_005070_4_0_9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000001412; 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: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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001412}.
FT DOMAIN 175..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 REGION 105..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 87961 MW; FF444011956D57FE CRC64;
MKLCSVCNKN VATIFTTRFE TGKPQIVGIC AECAKKMNIQ PLNQIIEAAG VTPEDMETYA
EQMNKLLDNM DINELLNNDL FSNMINNMNG MNMFKVQDDF IDKDKNEENT NSERNKDKSE
GNSNVKTRVK FKNKRRNLDK YAINLNDKAK DKKIDVVVGR DKEIERIIQI LNRRNKNNPI
LIGEPGVGKT AIAEGLAVKI IEKNVPIKLF DKEIYLLDLT SVVAGTQFRG QFEGRMKAIV
DEVTESENVI LVIDEVHNII GAGEAQGGAL NAANILKPAL ARGDIQVIGA TTLEEYRKYI
EKDSALERRF QPILVEEPSV KETIEILNNI KIYYEDYHKV KISKKIIEEA VKLSERYITD
RYLPDKAIDV IDEASSRVNL RNKNLVEFKI AKEELGELQN KMLNEANSGN YEKAAQYKTE
EYKLKNKVEE LEKKSKVELS VDDIAYVIEA WTKIPVQKVR EKEAEKLLNL EQRLHKRLIG
QDKAVRKLSR TIRRNRLGFK SKKRPASFIF VGPTGVGKTE LVRSLACELF GDEDSLIRID
MSEYMEKHTA SKLIGSPPGY VGYDEGGQLT EKIRRKPYSV VLLDEIEKAH PDIFNMLLQV
LEDGRLTDNQ GRTVFFDNSV IIMTSNLGTN FKESSIGFGN TNSIQIENSI KDALKETFKP
EFINRIDEIV IFEKLNKEEL YDIIDIMFDE VSEDLSEKNI KVHFTKEVKD FILKVGYDEK
YGARELKRAI QRYIEDEISE QYFRNEVKEG TNILVDIYEE SIYIKNM
//