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NORR_ALIF1
ID   NORR_ALIF1              Reviewed;         512 AA.
AC   Q5E3W8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Anaerobic nitric oxide reductase transcription regulator NorR {ECO:0000255|HAMAP-Rule:MF_01314};
GN   Name=norR {ECO:0000255|HAMAP-Rule:MF_01314}; OrderedLocusNames=VF_1783;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC   -!- FUNCTION: Required for the expression of anaerobic nitric oxide (NO)
CC       reductase, acts as a transcriptional activator for at least the norVW
CC       operon. Activation also requires sigma-54. {ECO:0000255|HAMAP-
CC       Rule:MF_01314}.
CC   -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC       {ECO:0000255|HAMAP-Rule:MF_01314}.
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DR   EMBL; CP000020; AAW86278.1; -; Genomic_DNA.
DR   RefSeq; WP_011262315.1; NC_006840.2.
DR   RefSeq; YP_205166.1; NC_006840.2.
DR   AlphaFoldDB; Q5E3W8; -.
DR   SMR; Q5E3W8; -.
DR   STRING; 312309.VF_1783; -.
DR   DNASU; 3279017; -.
DR   EnsemblBacteria; AAW86278; AAW86278; VF_1783.
DR   KEGG; vfi:VF_1783; -.
DR   PATRIC; fig|312309.11.peg.1809; -.
DR   eggNOG; COG3604; Bacteria.
DR   HOGENOM; CLU_000445_125_3_6; -.
DR   OMA; LRYEAHQ; -.
DR   OrthoDB; 123059at2; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000000537; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01314; NorR; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR023944; NorR.
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; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52540; SSF52540; 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   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Nucleotide-binding; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..512
FT                   /note="Anaerobic nitric oxide reductase transcription
FT                   regulator NorR"
FT                   /id="PRO_0000305628"
FT   DOMAIN          190..419
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01314"
FT   DNA_BIND        487..506
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01314"
FT   BINDING         218..225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01314"
FT   BINDING         281..290
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01314"
SQ   SEQUENCE   512 AA;  56767 MW;  623DCEFEE267AD82 CRC64;
     MKNIKDEWVQ IALDLTSGLS SKDRFERLLS TIRNALKCDA SALLLFKNQY FSPLATNGLD
     GDVIGRRFAI SQHPRLEAIA RAGDIVRFPS DSDLPDPYDG LIANEERQLQ VHSCIGLPLL
     VNERLIGAVT IDAFDPTQFD SFTNKELRII SALAATSLHT ALLMERLENQ SGENSNNSSF
     ERSPDNHVEM IGESLAMQEL QANINAVANT ELSVLITGET GVGKELVASA LHQRSTRAQQ
     NLVYLNCAAL PESVAESELF GHVKGAFTGA ISNRKGKFES ADNGTLFLDE IGELSLALQA
     KLLRVLQYGD IQRIGDDNHI KVNTRIIAAT NKTLSDEVKN GDFRADLYHR LSVFPIFVPP
     LRDRGNDVTL LVGYFAEKSR IKLAATSIRI TPEAITLLND YSWPGNIREL EHVISRAAVL
     SRAQSDDSDL VLSPTHFLIK KENHAEKNIA NQIVTPHSKN TKDLRSATDE FQANLIKKTY
     QEQQQNWAAT ARALQLDTGN LHRLAKRLNL KE
 
 
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