ID G3G7D9_STRSU Unreviewed; 419 AA.
AC G3G7D9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=ORFY {ECO:0000313|EMBL:AEP02669.1};
DE SubName: Full=Predicted transcriptional regulator of pyridoxine metabolism {ECO:0000313|EMBL:BAM94682.1};
OS Streptococcus suis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1307 {ECO:0000313|EMBL:AEP02669.1};
RN [1] {ECO:0000313|EMBL:AEP02669.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCTC10446 {ECO:0000313|EMBL:AEP02669.1};
RA Wang K.C., Fan W.X., Lu C.P.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAM94682.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCTC 10446 {ECO:0000313|EMBL:BAM94682.1};
RX PubMed=23416996; DOI=10.1128/AEM.03742-12;
RA Okura M., Takamatsu D., Maruyama F., Nozawa T., Nakagawa I., Osaki M.,
RA Sekizaki T., Gottschalk M., Kumagai Y., Hamada S.;
RT "Genetic analysis of capsular polysaccharide synthesis gene clusters from
RT all serotypes of Streptococcus suis: potential mechanisms for generation of
RT capsular variation.";
RL Appl. Environ. Microbiol. 79:2796-2806(2013).
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; JF791156; AEP02669.1; -; Genomic_DNA.
DR EMBL; AB737823; BAM94682.1; -; Genomic_DNA.
DR RefSeq; WP_024402814.1; NZ_CABEIV010000001.1.
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 1..69
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 419 AA; 49186 MW; 3248CBE60CFC2318 CRC64;
MKKYQVIIQD ILTGIEEHRF KRGEKLPSIR QLSEQYHCSK DTVQKAMLEL KYQNKIYAVE
KSGYYILEDR DFQDHTVELN PADFQELPYE DFRICLNESL IGRENYLFNY YHQQEGLAEL
ISSVQSLLMD YHVYTKKDHL VITAGSQQAL YILTQMETLA GKTEILIENP TYSRMIELIR
HQGIPYQTIE RDLDGIDLEE LESIFQTGKI KFFYTIPRLH NPLGSTYDIA TKTAIVKLAK
QYDVYIIEDD YLADFDSSHS LPLHYLDTDN RVIYIKSFTP TLFPALRIGA ISLPNQLRDT
FIKHKSLIDY DTNLIMQKAL SLYIDNGMFA RNTQHLHHIY HAQWNKIKDC LEKYALNIPF
RISKGSVTFQ LSKGILSPSI QHMFGKCYYF SGQKADFLQI FFEQDFADKL EQFVRYLNE
//
