DGAR_SALT1
ID DGAR_SALT1 Reviewed; 932 AA.
AC D0ZLR9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Transcriptional regulatory protein DagR {ECO:0000305};
DE AltName: Full=RpoN-dependent activator DgaR {ECO:0000303|PubMed:23836865};
DE Includes:
DE RecName: Full=Putative phosphotransferase EIIA component {ECO:0000305};
DE EC=2.7.1.- {ECO:0000255|PROSITE-ProRule:PRU00419};
DE AltName: Full=Putative PTS system EIIA component {ECO:0000305};
GN Name=dgaR; OrderedLocusNames=STM14_4550;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=23836865; DOI=10.1128/jb.00290-13;
RA Miller K.A., Phillips R.S., Mrazek J., Hoover T.R.;
RT "Salmonella utilizes D-glucosaminate via a mannose family
RT phosphotransferase system permease and associated enzymes.";
RL J. Bacteriol. 195:4057-4066(2013).
CC -!- FUNCTION: Involved in the regulation of the catabolism of D-
CC glucosaminate. {ECO:0000269|PubMed:23836865}.
CC -!- INDUCTION: Activated by D-glucosaminate and inhibited by D-glucose.
CC {ECO:0000269|PubMed:23836865}.
CC -!- DOMAIN: The PTS EIIA type-4 domain may serve a regulatory function,
CC through its phosphorylation activity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow with
CC D-glucosaminate as the sole carbon source.
CC {ECO:0000269|PubMed:23836865}.
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DR EMBL; CP001363; ACY90931.1; -; Genomic_DNA.
DR RefSeq; WP_001252662.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZLR9; -.
DR SMR; D0ZLR9; -.
DR EnsemblBacteria; ACY90931; ACY90931; STM14_4550.
DR KEGG; seo:STM14_4550; -.
DR PATRIC; fig|588858.6.peg.4147; -.
DR HOGENOM; CLU_014204_1_0_6; -.
DR OMA; VCAKSFL; -.
DR BioCyc; SENT588858:STM14_RS19930-MON; -.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.510; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011608; PRD.
DR InterPro; IPR036634; PRD_sf.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR002078; Sigma_54_int.
DR Pfam; PF00874; PRD; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53062; SSF53062; 1.
DR SUPFAM; SSF63520; SSF63520; 2.
DR PROSITE; PS51372; PRD_2; 2.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 2: Evidence at transcript level;
KW Activator; ATP-binding; DNA-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Phosphotransferase system; Repeat; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..932
FT /note="Transcriptional regulatory protein DagR"
FT /id="PRO_0000430796"
FT DOMAIN 111..343
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DOMAIN 462..567
FT /note="PRD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT DOMAIN 572..708
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT DOMAIN 835..932
FT /note="PRD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT ACT_SITE 580
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT BINDING 141..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 210..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 497
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT MOD_RES 870
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
SQ SEQUENCE 932 AA; 104936 MW; 3B98B74AEF0869C2 CRC64;
MRRIEIVLGE LERLTRGLCL ADLAQETAFT AEAIGFNLGL ARNSVSKDLN QLWNDGLAIK
SRGRPVYFLH RQALETLLGR QLEESEREVR SVADVLPHEE HYAPDDPFTS LIGYDRSLRD
AVEKGRAAVL YPHGLHVLLT GPSGVGKTFF AELMHRFACE QASGAIPPLV YFNCAEYAHN
PELLSSHLFG HRQGAFTGAN EHKTGLVEQA DGGYLLLDEV HRLSYEGQEK LFSILDKGEY
RPLGVSSQPR SISVRLICAT TEPVGSALLR TFQRRIQVCI DLPGIHQRSV EEQIELIVGF
LQRESRKIER TVSIDKPLLL WLLNKPLEGN IGQLKSDIQF LCAQAWASGM TEHNDTLQLD
KRLAEMSVNP TPEQRLLVDT LFEGKARLNI DARTLPALKT SLATGAEIEE SDLFYSFLTR
EYVNLRNSNV PPAETLAILK NKLSSIFEYG LYSRDSVAHP PRYGDQIEER VTLLIGCVEQ
VLGFSLPENL VNPLRKHFLA LIGYVQRGLI PQLYSSSLIL DRCKDEYDNA TLLCRKINEL
LHIQCPATEV VWLCLFLKEC RHYRQRIDAS PDCGVILIAH GATTATSQAQ YVNRVLEREL
FSAIDMPFEQ SVHDTLETLT QMIQTRQYRR LILLVDIGSL IHFGSTISKL FQIDVLLMPN
ITLTSLLEVG LDLSYETSDL PQLTALLQSK NIPCQLCTPQ QENGGKVLVI SCITGMGTAE
KIKKVLEESF GELMSQDTRM VILDYNEVRS LERVQQALNA SERLAGIVGT FQPGLPDIPF
ISLEELFSEQ GPELVLSLLT PDLSNAERRL EMERSAMRFI SALTMESIIN HISVLNPQRI
LKEMEGVFNH LTSSLSLKPS RQVTLRFLIH CCCMVERIVI NRKPLQMALE SQPNLDARAF
SVIKSAFLPI EDAYAIRLSD AEYFYIYELL YS
