GLNB_SYNP6
ID GLNB_SYNP6 Reviewed; 112 AA.
AC P0A3F5; P80016;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Nitrogen regulatory protein P-II;
DE AltName: Full=PII signal transducing protein;
GN Name=glnB; OrderedLocusNames=syc1192_d;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Inoue K., Bryant D.A.;
RT "Genes required for c-type cytochrome biogenesis.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
RN [3]
RP PROTEIN SEQUENCE OF 1-40.
RX PubMed=1653017; DOI=10.1016/s0005-2728(05)80206-3;
RA Li N., Warren P.V., Golbeck J.H., Frank G., Zuber H., Bryant D.A.;
RT "Polypeptide composition of the Photosystem I complex and the Photosystem I
RT core protein from Synechococcus sp. PCC 6301.";
RL Biochim. Biophys. Acta 1059:215-225(1991).
RN [4]
RP PROTEIN SEQUENCE OF 1-30.
RX PubMed=2110911; DOI=10.1016/0014-5793(90)80755-8;
RA Harrison M.A., Keen J.N., Findlay J.B.C., Allen J.F.;
RT "Modification of a glnB-like gene product by photosynthetic electron
RT transport in the cyanobacterium Synechococcus 6301.";
RL FEBS Lett. 264:25-28(1990).
CC -!- FUNCTION: P-II indirectly controls the transcription of the GS gene
CC (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-
CC phosphate, the transcriptional activator of glnA. When P-II is
CC phosphorylated, these events are reversed. In nitrogen-limiting
CC conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is
CC phosphorylated which allows the deadenylation of glutamine synthetase
CC (GS), thus activating the enzyme.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- PTM: Phosphorylation dependent on the nitrogen source and spectral
CC light quality. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; AF079137; AAF04333.1; -; Genomic_DNA.
DR EMBL; AP008231; BAD79382.1; -; Genomic_DNA.
DR PIR; A39696; A39696.
DR RefSeq; WP_011243504.1; NC_006576.1.
DR AlphaFoldDB; P0A3F5; -.
DR SMR; P0A3F5; -.
DR STRING; 269084.syc1192_d; -.
DR EnsemblBacteria; BAD79382; BAD79382; syc1192_d.
DR KEGG; syc:syc1192_d; -.
DR eggNOG; COG0347; Bacteria.
DR OMA; HQIEVNF; -.
DR Proteomes; UP000001175; Chromosome.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro.
DR Gene3D; 3.30.70.120; -; 1.
DR InterPro; IPR002187; N-reg_PII.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR InterPro; IPR017918; N-reg_PII_CS.
DR InterPro; IPR002332; N-reg_PII_urydylation_site.
DR PANTHER; PTHR30115; PTHR30115; 1.
DR Pfam; PF00543; P-II; 1.
DR PIRSF; PIRSF039144; GlnB; 1.
DR PRINTS; PR00340; PIIGLNB.
DR SMART; SM00938; P-II; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
DR PROSITE; PS00638; PII_GLNB_CTER; 1.
DR PROSITE; PS51343; PII_GLNB_DOM; 1.
DR PROSITE; PS00496; PII_GLNB_UMP; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein;
KW Transcription; Transcription regulation.
FT CHAIN 1..112
FT /note="Nitrogen regulatory protein P-II"
FT /id="PRO_0000139793"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ SEQUENCE 112 AA; 12391 MW; 5F44B64CBFF3C559 CRC64;
MKKIEAIIRP FKLDEVKIAL VNAGIVGMTV SEVRGFGRQK GQTERYRGSE YTVEFLQKLK
LEIVVEDAQV DTVIDKIVAA ARTGEIGDGK IFVSPVDQTI RIRTGEKNAD AI
