NTRB_ECO57
ID NTRB_ECO57 Reviewed; 349 AA.
AC P0AFB6; P06712;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Sensory histidine kinase/phosphatase NtrB {ECO:0000250|UniProtKB:P0AFB5};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P0AFB5};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:P0AFB5};
DE AltName: Full=Nitrogen regulation protein NR(II) {ECO:0000250|UniProtKB:P0AFB5};
DE AltName: Full=Nitrogen regulator II {ECO:0000250|UniProtKB:P0AFB5};
DE Short=NRII {ECO:0000250|UniProtKB:P0AFB5};
GN Name=glnL; OrderedLocusNames=Z5405, ECs4791;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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:0000250|UniProtKB:P0AFB5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P0AFB5};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AFB5}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P0AFB5}.
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DR EMBL; AE005174; AAG59058.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38214.1; -; Genomic_DNA.
DR PIR; F86074; F86074.
DR PIR; G91227; G91227.
DR RefSeq; NP_312818.1; NC_002695.1.
DR RefSeq; WP_000190577.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AFB6; -.
DR SMR; P0AFB6; -.
DR STRING; 155864.EDL933_5188; -.
DR EnsemblBacteria; AAG59058; AAG59058; Z5405.
DR EnsemblBacteria; BAB38214; BAB38214; ECs_4791.
DR GeneID; 60902695; -.
DR GeneID; 66672225; -.
DR GeneID; 915104; -.
DR KEGG; ece:Z5405; -.
DR KEGG; ecs:ECs_4791; -.
DR PATRIC; fig|386585.9.peg.5005; -.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_114_39_6; -.
DR OMA; EIMLTTA; -.
DR BRENDA; 2.7.13.3; 2026.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:UniProt.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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 3: Inferred from homology;
KW 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_0000074821"
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"
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
