NTRB_SALTI
ID NTRB_SALTI Reviewed; 349 AA.
AC P0A2E0; P41788;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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; Synonyms=ntrB; OrderedLocusNames=STY3875, t3615;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD03094.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71116.1; -; Genomic_DNA.
DR RefSeq; NP_458043.1; NC_003198.1.
DR RefSeq; WP_000146194.1; NZ_WSUR01000010.1.
DR AlphaFoldDB; P0A2E0; -.
DR SMR; P0A2E0; -.
DR STRING; 220341.16504731; -.
DR EnsemblBacteria; AAO71116; AAO71116; t3615.
DR KEGG; stt:t3615; -.
DR KEGG; sty:STY3875; -.
DR PATRIC; fig|220341.7.peg.3953; -.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_114_39_6; -.
DR OMA; EIMLTTA; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Kinase; Nitrogen fixation;
KW Nucleotide-binding; Phosphoprotein; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..349
FT /note="Sensory histidine kinase/phosphatase NtrB"
FT /id="PRO_0000074822"
FT DOMAIN 5..78
FT /note="PAS"
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; 38542 MW; 27002E40B6079A88 CRC64;
MASGIQPDAG QILNSLINSV LVVDDALAIH YANPAAQQLL AQSSRKLFGT PLPELLSYFS
LNIDLMRESL AAGQGFTDNE VTLVIDSRSH ILSLTAQRLP DDFILLEMAP MDNQRRLSQE
QLQHAQQIAA RDLVRGLAHE IKNPLGGLRG AAQLLSKALP DPALTEYTKV IIEQADRLRN
LVDRLLGPQH PGMHITESIH KVAERVVALV SMELPDNVRL IRDYDPSLPE LPHDPEQIEQ
VLLNIVRNAL QALGPEGGEI TLRTRTAFQL TLHGERYRLA ARIDVEDNGP GIPPHLQDTL
FYPMVSGREG GTGLGLSIAR NLIDQHAGKI EFTSWPGHTE FSVYLPIRK
