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NIFA_RHIME
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   03-AUG-2022, entry version 153.
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; Hyphomicrobiales;
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., Ausubel F.M.;
RT   "Nitrogen fixation specific regulatory genes of Klebsiella pneumoniae and
RT   Rhizobium meliloti share homology with the general nitrogen regulatory gene
RT   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) of
RT   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., Barloy-Hubler F.,
RA   Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA   Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA   Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA   Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT   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., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   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   -!- SEQUENCE CAUTION:
CC       Sequence=CAA26471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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   RefSeq; WP_010967431.1; NC_003037.1.
DR   AlphaFoldDB; P03028; -.
DR   SMR; P03028; -.
DR   PRIDE; P03028; -.
DR   EnsemblBacteria; AAK65101; AAK65101; SMa0815.
DR   GeneID; 61599254; -.
DR   KEGG; sme:SMa0815; -.
DR   PATRIC; fig|266834.11.peg.456; -.
DR   HOGENOM; CLU_000445_95_2_5; -.
DR   OMA; QAPIYIS; -.
DR   Proteomes; UP000001976; Plasmid pSymA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; 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   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; 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   4: Predicted;
KW   Activator; ATP-binding; DNA-binding; Metal-binding; Nitrogen fixation;
KW   Nucleotide-binding; Plasmid; Reference proteome; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..541
FT                   /note="Nif-specific regulatory protein"
FT                   /id="PRO_0000081313"
FT   DOMAIN          23..158
FT                   /note="GAF"
FT   DOMAIN          200..428
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        513..532
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          170..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..498
FT                   /note="Inter-domain linker"
FT   REGION          499..541
FT                   /note="C-terminal DNA-binding domain"
FT   BINDING         228..235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         291..300
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         442
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P05407"
FT   BINDING         447
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P05407"
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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