ID   NTRC_AZOBR     STANDARD;      PRT;   481 AA.
AC   P45671;
DT   01-NOV-1995 (Rel. 32, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Nitrogen assimilation regulatory protein.
GN   Name=ntrC;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sp7 / ATCC 29145;
RX   MEDLINE=96002420; PubMed=7553451;
RA   Machado H.B., Yates M.G., Funayama S., Rigo L.U., Steffens M.B.R.,
RA   Souza E.M., Pedrosa F.O.;
RT   "The ntrBC genes of Azospirillum brasilense are part of a nifR3-like-
RT   ntrB-ntrC operon and are negatively regulated.";
RL   Can. J. Microbiol. 41:674-684(1995).
CC   -!- FUNCTION: Member of the two-component regulatory system ntrB/ntrC
CC       involved in the activation of nitrogen assimilatory genes such as
CC       glnA. NtrC is phosphorylated by ntrB and interacts with sigma-54.
CC   -!- SIMILARITY: Contains 1 response regulatory domain.
CC   -!- SIMILARITY: Contains 1 sigma-54 factor interaction ATP-binding
CC       domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; Z37984; CAA86065.1; -.
DR   PIR; I39494; I39494.
DR   HSSP; P11028; 1ETY.
DR   InterPro; IPR003593; AAA_ATPase.
DR   InterPro; IPR011006; CheY_like.
DR   InterPro; IPR009057; Homeodomain_like.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR010114; NtrC.
DR   InterPro; IPR008298; Res_reg_NtrC.
DR   InterPro; IPR001789; Response_reg.
DR   InterPro; IPR002078; Sig54_interact.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PIRSF; PIRSF003187; Res_reg_NtrC; 1.
DR   PRINTS; PR01590; HTHFIS.
DR   ProDom; PD000039; Response_reg; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00448; REC; 1.
DR   TIGRFAMs; TIGR01199; HTH_fis; 1.
DR   TIGRFAMs; TIGR01818; ntrC; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; FALSE_NEG.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
KW   Activator; ATP-binding; DNA-binding; Nitrogen fixation;
KW   Phosphorylation; Repressor; Sensory transduction;
KW   Transcription regulation; Two-component regulatory system.
FT   DOMAIN        1    119       Response regulatory.
FT   DOMAIN      141    369       Sigma-54 factor interaction (Potential).
FT   NP_BIND     169    176       ATP (Potential).
FT   NP_BIND     232    241       ATP (Potential).
FT   DNA_BIND    451    470       H-T-H motif (By similarity).
FT   MOD_RES      54     54       4-aspartylphosphate (By similarity).
SQ   SEQUENCE   481 AA;  53309 MW;  9F117927E124146E CRC64;
     MSAATILVAD DDRAIRTVLT QALARLGHEV RTTGNASTLW RWVADGQGDL IITDVVMPDE
     NGLDLIPRIK KIRPDLRIIV MSAQNTLITA VKAAERGAFE YLPKPFDLKE LVSVVERALN
     SNTPPAALPA DAGEADEQLP LIGRSPAMQE IYRVLARLMG TDLTVTITGE SGTGKELVAR
     ALHDYGKRRN GPFVAINMAA IPRELIESEL FGHEKGAFTG ATNRSTGRFE QAQGGTLFLD
     EIGDMPLEAQ TRLLRVLQEG EYTTVGGRTP IKTDVRIVAA THRDLRTLIR QGLFREDLFY
     RLCVVPIRLP PLRERTEDVP LLVRHFLNQC SAQGLPVKSI DQPAMDRLKR YRWPGNVREL
     ENLVRRLAAL YSQEVIGLDV VEAELADTTP AAQPVEEPQG EGLSAAVERH LKDYFAAHKD
     GMPSNGLYDR VLREVERPLI SLSLSATRGN QIKAAQLLGL NRNTLRKKIR DLDIQVVRGL
     K
//