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Database: UniProt
Entry: P03028
LinkDB: P03028
Original site: P03028 
ID   NIFA_RHIME              Reviewed;         541 AA.
AC   P03028;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   19-FEB-2014, entry version 115.
DE   RecName: Full=Nif-specific regulatory protein;
GN   Name=nifA; Synonyms=fixD; OrderedLocusNames=RA0443; ORFNames=SMa0815;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymA (megaplasmid 1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2989799; DOI=10.1093/nar/13.12.4539;
RA   Buikema W.J., Szeto W.W., Lemley P.V., Orme-Johnson W.H.,
RA   Ausubel F.M.;
RT   "Nitrogen fixation specific regulatory genes of Klebsiella pneumoniae
RT   and Rhizobium meliloti share homology with the general nitrogen
RT   regulatory gene ntrC of K. pneumoniae.";
RL   Nucleic Acids Res. 13:4539-4555(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Weber G., Reilaender H., Puehler A.;
RT   "Mapping and expression of a regulatory nitrogen fixation gene (fixD)
RT   of Rhizobium meliloti.";
RL   Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481432; DOI=10.1073/pnas.161294798;
RA   Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P.,
RA   Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J.,
RA   Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L.,
RA   Kalman S., Keating D.H., Palm C., Peck M.C., Surzycki R., Wells D.H.,
RA   Yeh K.-C., Davis R.W., Federspiel N.A., Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire
RT   Sinorhizobium meliloti pSymA megaplasmid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F.,
RA   Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M.,
RA   Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D.,
RA   Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V.,
RA   Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B.,
RA   Ramsperger U., Surzycki R., Thebault P., Vandenbol M.,
RA   Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
CC   -!- FUNCTION: Required for activation of most nif operons, which are
CC       directly involved in nitrogen fixation.
CC   -!- SUBUNIT: Interacts with sigma-54.
CC   -!- SIMILARITY: Contains 1 GAF domain.
CC   -!- SIMILARITY: Contains 1 sigma-54 factor interaction domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA26471.1; Type=Erroneous initiation;
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DR   EMBL; X02615; CAA26470.1; -; Genomic_DNA.
DR   EMBL; X02615; CAA26471.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X03065; CAA26869.1; -; Genomic_DNA.
DR   EMBL; AE006469; AAK65101.2; -; Genomic_DNA.
DR   PIR; A03563; RGZRAM.
DR   PIR; C95317; C95317.
DR   RefSeq; NP_435689.2; NC_003037.1.
DR   ProteinModelPortal; P03028; -.
DR   STRING; 266834.SMa0815; -.
DR   ProMEX; P03028; -.
DR   EnsemblBacteria; AAK65101; AAK65101; SMa0815.
DR   GeneID; 1235479; -.
DR   KEGG; sme:SMa0815; -.
DR   PATRIC; 23627354; VBISinMel96828_0456.
DR   eggNOG; COG3604; -.
DR   HOGENOM; HOG000058487; -.
DR   KO; K02584; -.
DR   OrthoDB; EOG6WHNMG; -.
DR   ProtClustDB; CLSK807607; -.
DR   BioCyc; SMEL266834:GJF6-5448-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; 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; 1.10.10.60; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR010113; Nif-specific_regulatory_prot.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR01590; HTHFIS.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01817; nifA; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   1: Evidence at protein level;
KW   Activator; ATP-binding; Complete proteome; DNA-binding; Metal-binding;
KW   Nitrogen fixation; Nucleotide-binding; Plasmid; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN         1    541       Nif-specific regulatory protein.
FT                                /FTId=PRO_0000081313.
FT   DOMAIN       23    158       GAF.
FT   DOMAIN      200    428       Sigma-54 factor interaction.
FT   NP_BIND     228    235       ATP (Potential).
FT   NP_BIND     291    300       ATP (Potential).
FT   DNA_BIND    513    532       H-T-H motif (By similarity).
FT   REGION      429    498       Inter-domain linker.
FT   REGION      499    541       C-terminal DNA-binding domain.
FT   METAL       442    442       By similarity.
FT   METAL       447    447       By similarity.
SQ   SEQUENCE   541 AA;  59865 MW;  BC82DD9710A98A02 CRC64;
     MRKQDKRSAE IYSISKALMA PTRLETTLNN FVNTLSLILR MRRGGLEIPA SEGETKITAA
     TRNSGSPSAA DYTVPKAAID QVMTAGRLVV PDVCNSELFK DQIKWRGIGP TAFIAAAVEV
     DHETGGMLWF ECAEESDYDY EEEVHFLSMA ANLAGRAIRL HRTISRRERT FAEEQQEQQN
     SRDEQSQSSA RQRLLKNDGI IGESTALMTA VDTAKVMAET NSIVLLRGET GTGKECFAKL
     IHQHSTRQKK PFIKFNCPAL SESLLESELF GHEKGAFTGA IAQRVGRFES ANGGTLLLDE
     IGEIPPAFQA KLLRVIQEGE FERVGGTKTL KVDVRLIFAT NKDLEMAVQN GEFREDLYYR
     ISGVPLILPP LRHRDGDIPL LARAFLQRFN EENGRDLHFA PSALDHLSKC KFPGNVRELE
     NCVRRTATLA RSKTITSSDF ACQTDQCFSS RLWKGVHCSH GHIEIDAPAG TTPLLGAPAN
     DVPPKEPGSA GVASNLIERD RLISALEEAG WNQAKAARIL EKTPRQVGYA LRRHGVDVRK
     L
//
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