GenomeNet

Database: UniProt
Entry: P0AF29
LinkDB: P0AF29
Original site: P0AF29 
ID   NARL_ECOL6              Reviewed;         216 AA.
AC   P0AF29; P10957;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   29-OCT-2014, entry version 64.
DE   RecName: Full=Nitrate/nitrite response regulator protein NarL;
GN   Name=narL; OrderedLocusNames=c1681;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: This protein activates the expression of the nitrate
CC       reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons
CC       and represses the transcription of the fumarate reductase
CC       (frdABCD) operon in response to a nitrate/nitrite induction signal
CC       transmitted by either the NarX or NarQ proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Contains 1 HTH luxR-type DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00411}.
CC   -!- SIMILARITY: Contains 1 response regulatory domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00169}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN80148.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE014075; AAN80148.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_753586.1; NC_004431.1.
DR   ProteinModelPortal; P0AF29; -.
DR   SMR; P0AF29; 5-216.
DR   STRING; 199310.c1681; -.
DR   PRIDE; P0AF29; -.
DR   EnsemblBacteria; AAN80148; AAN80148; c1681.
DR   GeneID; 1035460; -.
DR   KEGG; ecc:c1681; -.
DR   PATRIC; 18281282; VBIEscCol75197_1562.
DR   HOGENOM; HOG000034813; -.
DR   KO; K07684; -.
DR   OMA; GEASHGE; -.
DR   OrthoDB; EOG69GZGV; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR011991; WHTH_DNA-bd_dom.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS00622; HTH_LUXR_1; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; Complete proteome; DNA-binding;
KW   Nitrate assimilation; Nucleotide-binding; Phosphoprotein; Repressor;
KW   Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN         1    216       Nitrate/nitrite response regulator
FT                                protein NarL.
FT                                /FTId=PRO_0000081147.
FT   DOMAIN        8    124       Response regulatory.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00169}.
FT   DOMAIN      149    214       HTH luxR-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00411}.
FT   DNA_BIND    173    192       H-T-H motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00411}.
FT   MOD_RES      59     59       4-aspartylphosphate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00169}.
SQ   SEQUENCE   216 AA;  23927 MW;  7DED78E4EF7EC57D CRC64;
     MSNQEPATIL LIDDHPMLRT GVKQLISMAP DITVVGEASN GEQGIELAES LDPDLILLDL
     NMPGMNGLET LDKLREKSLS GRIVVFSVSN HEEDVVTALK RGADGYLLKD MEPEDLLKAL
     HQAAAGEMVL SEALTPVLAA SLRANRATTE RDVNQLTPRE RDILKLIAQG LPNKMIARRL
     DITESTVKVH VKHMLKKMKL KSRVEAAVWV HQERIF
//
DBGET integrated database retrieval system