NTRB_ECOLI
ID NTRB_ECOLI Reviewed; 349 AA.
AC P0AFB5; P06712; Q2M8G6;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Sensory histidine kinase/phosphatase NtrB {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000269|PubMed:10074086, ECO:0000269|PubMed:2574599};
DE EC=3.1.3.- {ECO:0000269|PubMed:10074086, ECO:0000269|PubMed:2574599};
DE AltName: Full=Nitrogen regulation protein NR(II) {ECO:0000305};
DE AltName: Full=Nitrogen regulator II {ECO:0000303|PubMed:2574599};
DE Short=NRII {ECO:0000303|PubMed:2574599};
GN Name=glnL {ECO:0000303|PubMed:6148334};
GN Synonyms=glnR, ntrB {ECO:0000303|PubMed:2882477};
GN OrderedLocusNames=b3869, JW3840;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2882477; DOI=10.1093/nar/15.6.2757;
RA Miranda-Rios J., Sanchez-Pescador R., Urdea M., Covarrubias A.A.;
RT "The complete nucleotide sequence of the glnALG operon of Escherichia coli
RT K12.";
RL Nucleic Acids Res. 15:2757-2770(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=6148334; DOI=10.1128/jb.160.1.379-384.1984;
RA Ueno-Nishio S., Mango S., Reitzer L.J., Magasanik B.;
RT "Identification and regulation of the glnL operator-promoter of the complex
RT glnALG operon of Escherichia coli.";
RL J. Bacteriol. 160:379-384(1984).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RX PubMed=2865194; DOI=10.1016/0378-1119(85)90261-6;
RA Rocha M., Vazquez M., Garciarrubio A., Covarrubias A.A.;
RT "Nucleotide sequence of the glnA-glnL intercistronic region of Escherichia
RT coli.";
RL Gene 37:91-99(1985).
RN [7]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=2874557; DOI=10.1073/pnas.83.16.5909;
RA Ninfa A.J., Magasanik B.;
RT "Covalent modification of the glnG product, NRI, by the glnL product, NRII,
RT regulates the transcription of the glnALG operon in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5909-5913(1986).
RN [8]
RP FUNCTION.
RX PubMed=3304660; DOI=10.1016/0092-8674(87)90170-x;
RA Ninfa A.J., Reitzer L.J., Magasanik B.;
RT "Initiation of transcription at the bacterial glnAp2 promoter by purified
RT E. coli components is facilitated by enhancers.";
RL Cell 50:1039-1046(1987).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND ACTIVITY REGULATION.
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 PHOSPHORYLATION AT HIS-139.
RX PubMed=2016302; DOI=10.1016/s0021-9258(20)89585-4;
RA Ninfa A.J., Bennett R.L.;
RT "Identification of the site of autophosphorylation of the bacterial protein
RT kinase/phosphatase NRII.";
RL J. Biol. Chem. 266:6888-6893(1991).
RN [11]
RP ACTIVITY REGULATION.
RX PubMed=7961766; DOI=10.1016/s0021-9258(18)46926-8;
RA Atkinson M.R., Kamberov E.S., Weiss R.L., Ninfa A.J.;
RT "Reversible uridylylation of the Escherichia coli PII signal transduction
RT protein regulates its ability to stimulate the dephosphorylation of the
RT transcription factor nitrogen regulator I (NRI or NtrC).";
RL J. Biol. Chem. 269:28288-28293(1994).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PHOSPHORYLATION.
RX PubMed=10074086; DOI=10.1128/jb.181.6.1906-1911.1999;
RA Jiang P., Ninfa A.J.;
RT "Regulation of autophosphorylation of Escherichia coli nitrogen regulator
RT II by the PII signal transduction protein.";
RL J. Bacteriol. 181:1906-1911(1999).
RN [13]
RP ACTIVITY REGULATION.
RX PubMed=10231487; DOI=10.1046/j.1365-2958.1999.01349.x;
RA Atkinson M.R., Ninfa A.J.;
RT "Characterization of the GlnK protein of Escherichia coli.";
RL Mol. Microbiol. 32:301-313(1999).
RN [14] {ECO:0007744|PDB:1R62}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 190-349 OF MUTANT ASN-302,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=15157101; DOI=10.1021/bi049474r;
RA Song Y., Peisach D., Pioszak A.A., Xu Z., Ninfa A.J.;
RT "Crystal structure of the C-terminal domain of the two-component system
RT transmitter protein nitrogen regulator II (NRII; NtrB), regulator of
RT nitrogen assimilation in Escherichia coli.";
RL Biochemistry 43:6670-6678(2004).
CC -!- FUNCTION: Member of the two-component regulatory system NtrB/NtrC,
CC which controls expression of the nitrogen-regulated (ntr) genes in
CC response to nitrogen limitation. Under conditions of nitrogen
CC limitation, NtrB autophosphorylates and transfers the phosphoryl group
CC to NtrC. In the presence of nitrogen, acts as a phosphatase that
CC dephosphorylates and inactivates NtrC. {ECO:0000269|PubMed:10074086,
CC ECO:0000269|PubMed:2574599, ECO:0000269|PubMed:2874557,
CC ECO:0000269|PubMed:3304660}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:10074086,
CC ECO:0000269|PubMed:2574599};
CC -!- ACTIVITY REGULATION: The phosphatase and kinase activities are
CC regulated by the nitrogen regulatory proteins P-II 1 (GlnB) and P-II 2
CC (GlnK) (PubMed:2874557, PubMed:2574599, PubMed:10074086,
CC PubMed:10231487). GlnB acts by binding to NtrB, leading to activation
CC of the phosphatase activity and inhibition of the kinase activity.
CC Binding of GlnB to NtrB is allosterically controlled by the small-
CC molecule effector 2-ketoglutarate. At low 2-ketoglutarate
CC concentrations, GlnB interacts with NtrB, but not at high 2-
CC ketoglutarate concentrations (PubMed:10074086). Uridylylation of GlnB
CC also prevents interaction with NtrB (PubMed:7961766).
CC {ECO:0000269|PubMed:10074086, ECO:0000269|PubMed:10231487,
CC ECO:0000269|PubMed:2574599, ECO:0000269|PubMed:2874557,
CC ECO:0000269|PubMed:7961766}.
CC -!- INTERACTION:
CC P0AFB5; P0A9Z1: glnB; NbExp=5; IntAct=EBI-701156, EBI-551053;
CC P0AFB5; P0AFB8: glnG; NbExp=3; IntAct=EBI-701156, EBI-1113197;
CC P0AFB5; P0AC55: glnK; NbExp=5; IntAct=EBI-701156, EBI-559503;
CC P0AFB5; P0AFB5: glnL; NbExp=3; IntAct=EBI-701156, EBI-701156;
CC P0AFB5; P09153: tfaE; NbExp=4; IntAct=EBI-701156, EBI-9133821;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15157101}.
CC -!- DOMAIN: The C-terminal ATP-binding domain is required for both kinase
CC and phosphatase activities and contains the GlnB binding site.
CC {ECO:0000269|PubMed:15157101}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:10074086,
CC ECO:0000269|PubMed:2016302, ECO:0000269|PubMed:2574599}.
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DR EMBL; X05173; CAA28807.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03003.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76866.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77440.1; -; Genomic_DNA.
DR EMBL; K02176; AAA23881.1; -; Genomic_DNA.
DR PIR; A30377; RGECGL.
DR RefSeq; NP_418305.1; NC_000913.3.
DR RefSeq; WP_000190577.1; NZ_STEB01000017.1.
DR PDB; 1R62; X-ray; 1.60 A; A=190-349.
DR PDBsum; 1R62; -.
DR AlphaFoldDB; P0AFB5; -.
DR SMR; P0AFB5; -.
DR BioGRID; 4262629; 18.
DR BioGRID; 852657; 10.
DR DIP; DIP-9784N; -.
DR IntAct; P0AFB5; 10.
DR STRING; 511145.b3869; -.
DR iPTMnet; P0AFB5; -.
DR jPOST; P0AFB5; -.
DR PaxDb; P0AFB5; -.
DR PRIDE; P0AFB5; -.
DR EnsemblBacteria; AAC76866; AAC76866; b3869.
DR EnsemblBacteria; BAE77440; BAE77440; BAE77440.
DR GeneID; 60902695; -.
DR GeneID; 66672225; -.
DR GeneID; 948360; -.
DR KEGG; ecj:JW3840; -.
DR KEGG; eco:b3869; -.
DR PATRIC; fig|1411691.4.peg.2842; -.
DR EchoBASE; EB0382; -.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_114_39_6; -.
DR InParanoid; P0AFB5; -.
DR OMA; EIMLTTA; -.
DR PhylomeDB; P0AFB5; -.
DR BioCyc; EcoCyc:PROTEIN-NRII; -.
DR BioCyc; MetaCyc:PROTEIN-NRII; -.
DR EvolutionaryTrace; P0AFB5; -.
DR PRO; PR:P0AFB5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0016774; F:phosphotransferase activity, carboxyl group as acceptor; IDA:EcoCyc.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:EcoCyc.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0090593; P:peptidyl-histidine autophosphorylation; IDA:EcoCyc.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:EcoCyc.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IMP:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:EcoCyc.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Hydrolase; Kinase; Nitrogen fixation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..349
FT /note="Sensory histidine kinase/phosphatase NtrB"
FT /id="PRO_0000074820"
FT DOMAIN 5..78
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 136..349
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 139
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000269|PubMed:2016302"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1R62"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:1R62"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1R62"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:1R62"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1R62"
FT HELIX 235..253
FT /evidence="ECO:0007829|PDB:1R62"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1R62"
FT STRAND 258..272
FT /evidence="ECO:0007829|PDB:1R62"
FT STRAND 275..288
FT /evidence="ECO:0007829|PDB:1R62"
FT HELIX 314..325
FT /evidence="ECO:0007829|PDB:1R62"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:1R62"
FT STRAND 338..348
FT /evidence="ECO:0007829|PDB:1R62"
SQ SEQUENCE 349 AA; 38556 MW; 8B6B3BB18B2E2E98 CRC64;
MATGTQPDAG QILNSLINSI LLIDDNLAIH YANPAAQQLL AQSSRKLFGT PLPELLSYFS
LNIELMQESL EAGQGFTDNE VTLVIDGRSH ILSVTAQRMP DGMILLEMAP MDNQRRLSQE
QLQHAQQVAA RDLVRGLAHE IKNPLGGLRG AAQLLSKALP DPSLLEYTKV IIEQADRLRN
LVDRLLGPQL PGTRVTESIH KVAERVVTLV SMELPDNVRL IRDYDPSLPE LAHDPDQIEQ
VLLNIVRNAL QALGPEGGEI ILRTRTAFQL TLHGERYRLA ARIDVEDNGP GIPPHLQDTL
FYPMVSGREG GTGLGLSIAR NLIDQHSGKI EFTSWPGHTE FSVYLPIRK
