PTSJ_SALTY
ID PTSJ_SALTY Reviewed; 430 AA.
AC P40193;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Vitamin B6 salvage pathway transcriptional repressor PtsJ {ECO:0000305|PubMed:27987384};
DE AltName: Full=HTH-type transcriptional regulatory protein PtsJ {ECO:0000305};
GN Name=ptsJ {ECO:0000303|PubMed:27987384}; OrderedLocusNames=STM2436;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7612925; DOI=10.3109/10425179509029354;
RA Titgemeyer F.M., Reizer J., Reizer A., Tang J., Parr T.R. Jr.,
RA Saier M.H. Jr.;
RT "Nucleotide sequence of the region between crr and cysM in Salmonella
RT typhimurium: five novel ORFs including one encoding a putative
RT transcriptional regulator of the phosphotransferase system.";
RL DNA Seq. 5:145-152(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, DNA-BINDING, DISRUPTION PHENOTYPE, INDUCTION, PLP-BINDING, AND
RP SUBUNIT.
RC STRAIN=LT2;
RX PubMed=27987384; DOI=10.1111/febs.13994;
RA Tramonti A., Milano T., Nardella C., di Salvo M.L., Pascarella S.,
RA Contestabile R.;
RT "Salmonella typhimurium PtsJ is a novel MocR-like transcriptional repressor
RT involved in regulating the vitamin B6 salvage pathway.";
RL FEBS J. 284:466-484(2017).
CC -!- FUNCTION: Acts as transcriptional repressor of the pdxK gene, encoding
CC a pyridoxal kinase involved in the vitamin B6 salvage pathway. Also
CC represses transcription of its own gene. Binds to the ptsJ-pdxK
CC intergenic region, but does not bind pdxY and pdxH promoters. Among all
CC six B6 vitamers, only pyridoxal 5'-phosphate (PLP) clearly binds to the
CC protein and acts as an effector molecule for PtsJ, inducing a protein
CC conformational change that increases affinity for DNA. Thus, PLP
CC stabilizes protein-DNA interactions, reinforcing repression.
CC {ECO:0000269|PubMed:27987384}.
CC -!- SUBUNIT: Homodimer in both apo- and holo-forms.
CC {ECO:0000269|PubMed:27987384}.
CC -!- INDUCTION: Represses its own expression. {ECO:0000269|PubMed:27987384}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display a 80-fold
CC increase in pdxK expression with respect to wild-type when grown in
CC minimal medium. A much lower but significant 2/3-fold increase of
CC expression is also observed for pdxY and pdxH.
CC {ECO:0000269|PubMed:27987384}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
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DR EMBL; U11243; AAC43344.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21330.1; -; Genomic_DNA.
DR RefSeq; NP_461371.1; NC_003197.2.
DR RefSeq; WP_000565119.1; NC_003197.2.
DR AlphaFoldDB; P40193; -.
DR SMR; P40193; -.
DR STRING; 99287.STM2436; -.
DR PaxDb; P40193; -.
DR DNASU; 1253958; -.
DR EnsemblBacteria; AAL21330; AAL21330; STM2436.
DR GeneID; 1253958; -.
DR KEGG; stm:STM2436; -.
DR PATRIC; fig|99287.12.peg.2574; -.
DR HOGENOM; CLU_017584_2_0_6; -.
DR OMA; VEDPGWA; -.
DR PhylomeDB; P40193; -.
DR BioCyc; SENT99287:STM2436-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.640.10; -; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF00392; GntR; 1.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Pyridoxal phosphate; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..430
FT /note="Vitamin B6 salvage pathway transcriptional repressor
FT PtsJ"
FT /id="PRO_0000050668"
FT DOMAIN 4..72
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT DNA_BIND 32..51
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT REGION 70..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 282
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P00509"
SQ SEQUENCE 430 AA; 46508 MW; 64E83333E109964F CRC64;
MIDGKTANEI FDSIRQHIIA GTLRAEDSLP PVRELASELK VNRNTVAAAY KRLITAGLAQ
SLGRNGTVIK GSPSPVALEG GDPHTPLHDL SGGNPDPQRL PDLSRYFARL SRTPHLYGDA
PVSPELHAWA ARWLRDATPV AGEIDITSGA IDAIERLLCA HLLPGDSVAV EDPCFLSSIN
MLRYAGFSAS PVSVDSEGMQ PEKLERALNQ GARAVILTPR AHNPTGCSLS ARRAAALQNM
LARYPQVVVI IDDHFALLSS SPWQPVIAQT TQHWAVIRSV SKTLGPDLRL AIVASDSATS
AKLRLRLNAG SQWVSHLLQD LVYACLTDPE YQHRLTQTRL FYAARQQKLA RALQQYGIAI
SPGDGVNAWL PLDTHSQATA FTLAKSGWLV REGEAFGVSA PSHGLRITLS TLNDSEINTL
AADIHQALNR
