ID B7MNJ7_ECO45 Unreviewed; 410 AA.
AC B7MNJ7;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Bifunctional DNA-binding transcriptional repressor and NMN adenylyltransferase {ECO:0000313|EMBL:CAR06210.1};
GN Name=nadR {ECO:0000313|EMBL:CAR06210.1};
GN OrderedLocusNames=ECS88_5071 {ECO:0000313|EMBL:CAR06210.1};
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR06210.1, ECO:0000313|Proteomes:UP000000747};
RN [1] {ECO:0000313|Proteomes:UP000000747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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DR EMBL; CU928161; CAR06210.1; -; Genomic_DNA.
DR RefSeq; WP_000093837.1; NC_011742.1.
DR AlphaFoldDB; B7MNJ7; -.
DR KEGG; ecz:ECS88_5071; -.
DR HOGENOM; CLU_052648_0_1_6; -.
DR Proteomes; UP000000747; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:InterPro.
DR GO; GO:0050262; F:ribosylnicotinamide kinase activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR CDD; cd00093; HTH_XRE; 1.
DR CDD; cd02019; NK; 1.
DR CDD; cd02167; NMNAT_NadR; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR016429; NAD_NadR.
DR InterPro; IPR038727; NadR/Ttd14_AAA_dom.
DR InterPro; IPR006417; NadR_NMN_Atrans.
DR InterPro; IPR041749; NMNAT_NadR.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR NCBIfam; TIGR01526; nadR_NMN_Atrans; 1.
DR PANTHER; PTHR37512:SF1; AAA_28 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR37512; TRIFUNCTIONAL NAD BIOSYNTHESIS/REGULATOR PROTEIN NADR; 1.
DR Pfam; PF13521; AAA_28; 1.
DR Pfam; PF01381; HTH_3; 1.
DR PIRSF; PIRSF004776; NadR_NMNAT/RNK; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000313|EMBL:CAR06210.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR004776-1};
KW Nucleotidyltransferase {ECO:0000313|EMBL:CAR06210.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000747};
KW Transferase {ECO:0000313|EMBL:CAR06210.1}.
FT DOMAIN 7..62
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
FT BINDING 70..73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT BINDING 77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT BINDING 104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT BINDING 144..157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT BINDING 177..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT BINDING 204..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT BINDING 259..261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
SQ SEQUENCE 410 AA; 47396 MW; CDCE14A117A7C700 CRC64;
MSSFDYLKTA IKQQGCTLQQ VADASGMTKG YLSQLLNAKI KSPSAQKLEA LHRYLGLEFP
RQKKTIGVVF GKFYPLHTGH IYLIQRACSQ VDELHIIMGF DYTRDRALFE DSAMSQQPTV
PDRLRWLLQT FKYQKNIRIH AFNEEGMEPY PHGWDVWSNG IKKFMAEKGI QPDLIYTSEE
ADAPQYMEHL GIETVLVDPK RTFMSISGAQ IRENPFRYWE YIPTEVKPFF VRTVAILGGE
SSGKSTLVNK LANIFNTTSA WEYGRDYVFS HLGGDEIALQ YSDYDKIALG HAQYIDFAVK
YANKVAFIDT DFVTTQAFCK KYEGREHPFV QALIDEYRFD LVILLENNTP WVADGLRSLG
SSVDRKEFQN LLVEMLEENN IEFVRVEEDD YDSRFLRCVE LVREMMGEQR
//
