ID B1KW73_CLOBM Unreviewed; 469 AA.
AC B1KW73;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Transcriptional regulator, GntR family/aminotransferase {ECO:0000313|EMBL:ACA54364.1};
GN OrderedLocusNames=CLK_0035 {ECO:0000313|EMBL:ACA54364.1};
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA54364.1, ECO:0000313|Proteomes:UP000000722};
RN [1] {ECO:0000313|EMBL:ACA54364.1, ECO:0000313|Proteomes:UP000000722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
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: In the C-terminal section; belongs to the class-I
CC pyridoxal-phosphate-dependent aminotransferase family.
CC {ECO:0000256|ARBA:ARBA00005384}.
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DR EMBL; CP000962; ACA54364.1; -; Genomic_DNA.
DR RefSeq; WP_012342481.1; NC_010520.1.
DR AlphaFoldDB; B1KW73; -.
DR KEGG; cbl:CLK_0035; -.
DR HOGENOM; CLU_017584_0_1_9; -.
DR Proteomes; UP000000722; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46577; HTH-TYPE TRANSCRIPTIONAL REGULATORY PROTEIN GABR; 1.
DR PANTHER; PTHR46577:SF1; HTH-TYPE TRANSCRIPTIONAL REGULATORY PROTEIN GABR; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF00392; GntR; 1.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 10..78
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 469 AA; 53718 MW; E211B324531913AB CRC64;
MLYIDRGSNI PIYQQIYEQM KQDIISGNLP VESRVISTRV LASELQVGRN SVENAYDQLR
LEGYITSIPG SGYIVNKLEF DLIQESPKEQ RQSKLLTEHL AVLPDKMKYS FQYGELDETN
FPKKLWRTYV ANVLDEPLAH SIHSYGDGKG DPQLRQQIKQ YLYHSRGVQC ETEQIILCSG
TQSALETIIR IFSGKKTVAM EEPCYDGARA VFQGNGFKIL PVPVREDGID LQKLSSQSIP
MVYLSPSHQF PTGAVMPIHN RMEVLNLARQ RDMMIIEDDY DSEFRYKGRP IPSLQSIDQA
GRVIYVGTFS KALSPGLRIS HLVLPTWLLA SYQEKYRGYQ CTIPLIEQRV LLHFMQDGHW
EKHIRRVCLS QKRKHDTLIA AIQQIIGDRV RVYGHHAGLH ILLEFVDGQQ EDTLVQKAMR
YGVQVNPISP FWLEKNCYSG NAVVLGYGKI KEKDIIPSVE LLNKAWFEE
//
