ID A0A140NIN5_PROSM Unreviewed; 410 AA.
AC A0A140NIN5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Bifunctional DNA-binding transcriptional repressor/ NMN adenylyltransferase {ECO:0000313|EMBL:AFH93339.1};
DE EC=2.7.7.1 {ECO:0000313|EMBL:AFH93339.1};
GN OrderedLocusNames=S70_07350 {ECO:0000313|EMBL:AFH93339.1};
OS Providencia stuartii (strain MRSN 2154).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1157951 {ECO:0000313|EMBL:AFH93339.1, ECO:0000313|Proteomes:UP000005012};
RN [1] {ECO:0000313|EMBL:AFH93339.1, ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|EMBL:AFH93339.1,
RC ECO:0000313|Proteomes:UP000005012};
RX PubMed=22740665; DOI=10.1128/JB.00615-12;
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete Genome Sequence of Providencia stuartii Clinical Isolate MRSN
RT 2154.";
RL J. Bacteriol. 194:3736-3737(2012).
RN [2] {ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|Proteomes:UP000005012};
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete genome sequence of Providencia stuartii clinical isolate MRSN
RT 2154.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003488; AFH93339.1; -; Genomic_DNA.
DR RefSeq; WP_004926682.1; NC_017731.1.
DR AlphaFoldDB; A0A140NIN5; -.
DR GeneID; 79055185; -.
DR KEGG; psi:S70_07350; -.
DR PATRIC; fig|1157951.4.peg.1467; -.
DR HOGENOM; CLU_052648_0_1_6; -.
DR OrthoDB; 3249147at2; -.
DR Proteomes; UP000005012; 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:UniProtKB-EC.
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 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; 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; PF01467; CTP_transf_like; 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:AFH93339.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR004776-1};
KW Nucleotidyltransferase {ECO:0000313|EMBL:AFH93339.1};
KW Transferase {ECO:0000313|EMBL:AFH93339.1}.
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; 47364 MW; 0202ADDDDE595C5C CRC64;
MAEFDYLKNA IKQAGYTLQQ VADASDMTKG YLSQLINNKI KSPSAQKIAA LHRFLGLEYP
NKQKSIGVVF GKFYPLHTGH IYLIQRACSQ VDELHVILCH DEPRDKDLFV NSSMSQQPTV
SDRLRWLLQT FKYQKNIHIH SFDEQGIEPY PHGWEVWSEG MKGFLKKHNI HPSFIYSGEA
NDAPRYKKYL GIETILIDPE RTFMNISGNQ IRQAPFRYWD YIPTEVKPFF VRKVAILGGE
SSGKSTLVNK LANIFNTTSA WEFGRDYVFS HLGGDEMALQ YSDYDKIALG HAQYIDFAVK
YANKVAFIDT DFITTQAFCK RYEGKEHPFV QALIDEYRFD LVILLENNTP WVADGLRSLG
SEKDRQEFQS LLIEMLKKNN VEFVHVDSPD YDTRFLTCIS LVQQLLMLDE
//
