GLNB_ECOLI
ID GLNB_ECOLI Reviewed; 112 AA.
AC P0A9Z1; P05826;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Nitrogen regulatory protein P-II 1;
GN Name=glnB; OrderedLocusNames=b2553, JW2537;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND URIDYLYLATION AT TYR-51.
RX PubMed=2885322; DOI=10.1016/s0021-9258(18)47469-8;
RA Son H.S., Rhee S.G.;
RT "Cascade control of Escherichia coli glutamine synthetase. Purification and
RT properties of PII protein and nucleotide sequence of its structural gene.";
RL J. Biol. Chem. 262:8690-8695(1987).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=2907369; DOI=10.1007/bf00331314;
RA Holtel A., Merrick M.;
RT "Identification of the Klebsiella pneumoniae glnB gene: nucleotide sequence
RT of wild-type and mutant alleles.";
RL Mol. Gen. Genet. 215:134-138(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2034230; DOI=10.1007/bf00273586;
RA Vasudevan S.G., Armarego W.L.F., Shaw D.C., Lilley P.E., Dixon N.E.,
RA Poole R.K.;
RT "Isolation and nucleotide sequence of the hmp gene that encodes a
RT haemoglobin-like protein in Escherichia coli K-12.";
RL Mol. Gen. Genet. 226:49-58(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8226691; DOI=10.1128/jb.175.22.7441-7449.1993;
RA Liu J., Magasanik B.;
RT "The glnB region of the Escherichia coli chromosome.";
RL J. Bacteriol. 175:7441-7449(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8412694; DOI=10.1111/j.1365-2958.1993.tb01706.x;
RA van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.;
RT "The genes of the glutamine synthetase adenylylation cascade are not
RT regulated by nitrogen in Escherichia coli.";
RL Mol. Microbiol. 9:443-458(1993).
RN [9]
RP REVIEW.
RX PubMed=2574599; DOI=10.1016/0300-9084(89)90104-1;
RA Magasanik B.;
RT "Regulation of transcription of the glnALG operon of Escherichia coli by
RT protein phosphorylation.";
RL Biochimie 71:1005-1012(1989).
RN [10]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=8293810; DOI=10.1016/0014-5793(94)80203-3;
RA Vasudevan S.G., Gedye C., Dixon N.E., Cheah E., Carr P.D., Suffolk P.M.,
RA Jeffrey P.D., Ollis D.L.;
RT "Escherichia coli PII protein: purification, crystallization and oligomeric
RT structure.";
RL FEBS Lett. 337:255-258(1994).
RN [11]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=7866749; DOI=10.1016/s0969-2126(94)00100-6;
RA Cheah E., Carr P.D., Suffolk P.M., Vasuvedan S.G., Dixon N.E., Ollis D.L.;
RT "Structure of the Escherichia coli signal transducing protein PII.";
RL Structure 2:981-990(1994).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=15299730; DOI=10.1107/s0907444995007293;
RA Carr P.D., Cheah E., Suffolk P.M., Vasudevan S.G., Dixon N.E., Ollis D.L.;
RT "X-ray structure of the signal transduction protein from Escherichia coli
RT at 1.9 A.";
RL Acta Crystallogr. D 52:93-104(1996).
CC -!- FUNCTION: P-II indirectly controls the transcription of the glutamine
CC synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-
CC I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II
CC is uridylylated to P-II-UMP, these events are reversed. When the ratio
CC of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP,
CC which causes the deadenylation of glutamine synthetase by GlnE, so
CC activating the enzyme.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:8293810}.
CC -!- INTERACTION:
CC P0A9Z1; P0A9Z1: glnB; NbExp=4; IntAct=EBI-551053, EBI-551053;
CC P0A9Z1; P27249: glnD; NbExp=3; IntAct=EBI-551053, EBI-552032;
CC P0A9Z1; P0AC55: glnK; NbExp=3; IntAct=EBI-551053, EBI-559503;
CC P0A9Z1; P0AFB5: glnL; NbExp=5; IntAct=EBI-551053, EBI-701156;
CC P0A9Z1; P0AF90: rraB; NbExp=3; IntAct=EBI-551053, EBI-544031;
CC -!- PTM: Uridylylated/deuridylylated by GlnD.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23883.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M16778; AAA23883.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X58872; CAA41683.1; -; Genomic_DNA.
DR EMBL; S67014; AAB28779.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75606.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16461.1; -; Genomic_DNA.
DR EMBL; Z21843; CAA79890.1; -; Genomic_DNA.
DR PIR; C49940; RGECP2.
DR RefSeq; NP_417048.1; NC_000913.3.
DR RefSeq; WP_000717694.1; NZ_STEB01000011.1.
DR PDB; 1PIL; X-ray; 2.70 A; A=1-112.
DR PDB; 2PII; X-ray; 1.90 A; A=1-112.
DR PDB; 5L9N; X-ray; 1.90 A; A=1-112.
DR PDBsum; 1PIL; -.
DR PDBsum; 2PII; -.
DR PDBsum; 5L9N; -.
DR AlphaFoldDB; P0A9Z1; -.
DR SMR; P0A9Z1; -.
DR BioGRID; 4259201; 40.
DR BioGRID; 851355; 6.
DR DIP; DIP-35005N; -.
DR IntAct; P0A9Z1; 18.
DR STRING; 511145.b2553; -.
DR jPOST; P0A9Z1; -.
DR PaxDb; P0A9Z1; -.
DR PRIDE; P0A9Z1; -.
DR EnsemblBacteria; AAC75606; AAC75606; b2553.
DR EnsemblBacteria; BAA16461; BAA16461; BAA16461.
DR GeneID; 63941229; -.
DR GeneID; 67416931; -.
DR GeneID; 947016; -.
DR KEGG; ecj:JW2537; -.
DR KEGG; eco:b2553; -.
DR PATRIC; fig|1411691.4.peg.4181; -.
DR EchoBASE; EB0379; -.
DR eggNOG; COG0347; Bacteria.
DR HOGENOM; CLU_082268_0_0_6; -.
DR InParanoid; P0A9Z1; -.
DR OMA; HQIEVNF; -.
DR PhylomeDB; P0A9Z1; -.
DR BioCyc; EcoCyc:PROTEIN-PII; -.
DR BioCyc; MetaCyc:PROTEIN-PII; -.
DR EvolutionaryTrace; P0A9Z1; -.
DR PRO; PR:P0A9Z1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0008047; F:enzyme activator activity; IDA:EcoCyc.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0036094; F:small molecule binding; IMP:EcoCyc.
DR GO; GO:0050790; P:regulation of catalytic activity; IDA:EcoCyc.
DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; IDA:EcoCyc.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IDA:EcoCyc.
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 3D-structure; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..112
FT /note="Nitrogen regulatory protein P-II 1"
FT /id="PRO_0000139771"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675,
FT ECO:0000269|PubMed:2885322"
FT CONFLICT 19
FT /note="A -> R (in Ref. 1; AAA23883)"
FT /evidence="ECO:0000305"
FT CONFLICT 81..82
FT /note="AQ -> E (in Ref. 1; AAA23883)"
FT /evidence="ECO:0000305"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2PII"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:2PII"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:2PII"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:2PII"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1PIL"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:2PII"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2PII"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:2PII"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2PII"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2PII"
SQ SEQUENCE 112 AA; 12425 MW; D1A4158A2F225042 CRC64;
MKKIDAIIKP FKLDDVREAL AEVGITGMTV TEVKGFGRQK GHTELYRGAE YMVDFLPKVK
IEIVVPDDIV DTCVDTIIRT AQTGKIGDGK IFVFDVARVI RIRTGEEDDA AI
