ID   NTRY_AZOBR     STANDARD;      PRT;   777 AA.
AC   P45675;
DT   01-NOV-1995 (Rel. 32, Created)
DT   28-FEB-2003 (Rel. 41, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Nitrogen regulation protein ntrY homolog (EC 2.7.3.-).
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;
RA   Ishida M.L.;
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 1-300.
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 ntrY/ntrX
CC       involved in nitrogen level control. Probably activates ntrX by
CC       phosphorylation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein (Potential).
CC   -!- SIMILARITY: Contains 1 HAMP domain.
CC   -!- SIMILARITY: Contains 1 histidine kinase domain.
CC   -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) dimerization 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; CAA86066.2; -.
DR   PIR; I39495; I39495.
DR   HSSP; P02933; 1BXD.
DR   InterPro; IPR003594; ATPbind_ATPase.
DR   InterPro; IPR004358; Bact_sens_pr_C.
DR   InterPro; IPR002048; EF-hand.
DR   InterPro; IPR003660; HAMP.
DR   InterPro; IPR009082; His_kin_homodim.
DR   InterPro; IPR003661; His_kinA_N.
DR   InterPro; IPR005467; His_kinase.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; FALSE_NEG.
KW   Kinase; Nitrogen fixation; Phosphorylation; Sensory transduction;
KW   Transferase; Transmembrane; Two-component regulatory system.
FT   TRANSMEM     29     49       Potential.
FT   TRANSMEM     61     81       Potential.
FT   TRANSMEM    107    127       Potential.
FT   TRANSMEM    202    222       Potential.
FT   TRANSMEM    305    325       Potential.
FT   DOMAIN      327    380       HAMP.
FT   DOMAIN      392    465       PAS.
FT   DOMAIN      523    745       Histidine kinase.
SQ   SEQUENCE   777 AA;  84353 MW;  23C524D2F0631D76 CRC64;
     MSPTPPETVT PLWQQFLRWA ARVGLAKRLA FALSLAALVA GFATYTALTE SAPFGETNPR
     TVTWLLTLDL ALLLLLGVLI ARRIVYLWIG RRRGLAGSQM HVRLVAVFSL LAVAPAIIMA
     IFSTVFFYVG VQSWFSERVR TAVNESLAVA SAYLHEHQQN IRADALAMAN DLNQEAARLA
     SDPERFEQVV ATQAMLRALS EAIVFNGTTG AIVARSGYTF ALEFDPIPDD KLATARRGEV
     AMIVSENDDR VRALVRLDRF ADTYLYVGRM VEPRVLSHMA SAEGAVREFG ALESQRGSLQ
     ITFTLIFLCV ALLLLLAAVW AGLIFATRLV RPISALIGAA DRVRAGDLTV RVTERPAEDD
     LALLSRAFNR MTTEIESQRH ALLSANRLID SRRRFTETVL SGVSAGRDGL DAEGRITLSK
     FSAARLLGVK DAESLIGMRL AELVPEMGGL LHEAPGRPGL VVQDQIKIRR DGTTPLTLLV
     RISTEGRGSG MMRGYVVTFD EHHRTWSPAQ RKAAWARRRP IAASPTRVKN PLTPIQLSAE
     PCAASTLKEI TSDTEVFTMC TDTIVRQVDD IRRMVDEFSA FARMPQPVMK PCNLNDLVRQ
     AVFLQSSAHA GKIKFDMALP QGPLTVPCDS RQISQALTNL LQNAADAIEG RPPPAEGTEL
     PPGHVAIRVE ADAERIAMII EDNGKGLPTE ERDRLTEPYV TTRAKGTGLG LAIVKKIMED
     HGGVLTLEDR EGGGARVGLV IPQHIPPASG TAAGDAPGGV GTPAETGEEK RHAAHGA
//