ID H3SI55_9BACL Unreviewed; 479 AA.
AC H3SI55;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:EHQ61244.1};
GN ORFNames=PDENDC454_16118 {ECO:0000313|EMBL:EHQ61244.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ61244.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ61244.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ61244.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC pyridoxal-phosphate-dependent aminotransferase family.
CC {ECO:0000256|ARBA:ARBA00005384}.
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:EHQ61244.1}.
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DR EMBL; AHKH01000043; EHQ61244.1; -; Genomic_DNA.
DR RefSeq; WP_006677717.1; NZ_AHKH01000043.1.
DR AlphaFoldDB; H3SI55; -.
DR STRING; 1131935.PDENDC454_16118; -.
DR PATRIC; fig|1131935.3.peg.3357; -.
DR OrthoDB; 9802601at2; -.
DR Proteomes; UP000003900; Unassembled WGS sequence.
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:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:SF2; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF00392; GntR; 1.
DR PRINTS; PR00035; HTHGNTR.
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 Reference proteome {ECO:0000313|Proteomes:UP000003900}.
FT DOMAIN 10..78
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 479 AA; 53467 MW; F810D1522510933F CRC64;
MWQPDRSSKQ PLYQQIAAYI EQRISYGEFP PGSLLPSERK FAEQINVNRS TVVQAYEELR
ASGMIESMVG SGTRVSKSRW GAAPKDMPDW LQYVDGGAAM HPHQSCLRLI RQELDSGRPL
IDFASGELSP DLSPNEAIRQ LLSEHALHED LGYDHPQGYV PLRQALASYL KQYRGIRATE
SSILVTSGSH QSLYLITKRL LSPGDAVAIE DPSYYYSLPM FHTAGLRLFR LPVDEKGVCP
EGILSLHREH QIRMIFVNPN YHNPTGRVLD PARRERLLEI CGHLGIPIVE DDPFSLTSFT
GNPPPSLKSN DAGSTVLYIG SLSKIVASGL RIGWMVAPQS VVSRLTDEKQ QMDFGLSVLP
QRIAAQLLAS AHFEGHLLRL RKELSHKRNL LLDALHRELP GELSYTLPQG GLHLWCRMRR
PVDDDRLLEE GLRRGVVFVP GSVYGSEPGY VRFTFARPQP GQIGRGIALF AEALRAAGR
//