ID   GLNB_AZOBR     STANDARD;      PRT;   112 AA.
AC   P21193;
DT   01-MAY-1991 (Rel. 18, Created)
DT   01-MAY-1991 (Rel. 18, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Nitrogen regulatory protein P-II.
GN   Name=glnB;
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=91094780; PubMed=1702507;
RA   de Zamaroczy M., Delorme F., Elmerich C.;
RT   "Characterization of three different nitrogen-regulated promoter
RT   regions for the expression of glnB and glnA in Azospirillum
RT   brasilense.";
RL   Mol. Gen. Genet. 224:421-430(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 88-112.
RC   STRAIN=Sp7 / ATCC 29145;
RX   MEDLINE=87076765; PubMed=2878685;
RA   Bozouklian H., Elmerich C.;
RT   "Nucleotide sequence of the Azospirillum brasilense Sp7 glutamine
RT   synthetase structural gene.";
RL   Biochimie 68:1181-1187(1986).
CC   -!- FUNCTION: In nitrogen-limiting conditions, when the ratio of Gln
CC       to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-
CC       II-UMP allows the deadenylylation of glutamine synthetase (GS),
CC       thus activating the enzyme. Converserly, in nitrogen excess P-II
CC       is deuridylated and promotes the adenylation of GS.
CC   -!- FUNCTION: P-II indirectly controls the transcription of the GS
CC       gene (glnA). P-II prevents NR-II catalyzed conversion of NR-I to
CC       NR-I-phosphate, the transcriptional activator of glnA. When P-II
CC       is uridylylated to P-II-UMP, these events are reversed.
CC   -!- SUBUNIT: Homotrimer (By similarity).
CC   -!- SIMILARITY: Belongs to the P(II) protein family.
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; X51499; CAA35867.1; -.
DR   EMBL; M26107; -; NOT_ANNOTATED_CDS.
DR   PIR; S13078; S13078.
DR   HSSP; P05826; 2PII.
DR   InterPro; IPR002187; PII_glnB.
DR   InterPro; IPR002332; PII_GlnB_UMP_S.
DR   Pfam; PF00543; P-II; 1.
DR   PRINTS; PR00340; PIIGLNB.
DR   ProDom; PD001194; PII_glnB; 1.
DR   PROSITE; PS00638; PII_GLNB_CTER; 1.
DR   PROSITE; PS00496; PII_GLNB_UMP; 1.
KW   Nitrogen fixation; Transcription regulation.
FT   BINDING      51     51       UMP (covalent) (By similarity).
SQ   SEQUENCE   112 AA;  12371 MW;  B6258EC9C4B63871 CRC64;
     MKKIEAIIKP FKLDEVKEAL HEVGIKGITV TEAKGFGRQK GHTELYRGAE YVVDFLPKVK
     IEVVMEDSLV ERAIEAIQQA AHTGRIGDGK IFVTPVEEVV RIRTGEKGGD AI
//