NTRB_SALTY
ID NTRB_SALTY Reviewed; 349 AA.
AC P0A2D9; P41788;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=STM4006;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Kustu S.G.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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; X85104; CAA59424.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22845.1; -; Genomic_DNA.
DR PIR; S53023; S53023.
DR RefSeq; NP_462886.1; NC_003197.2.
DR RefSeq; WP_000146194.1; NC_003197.2.
DR AlphaFoldDB; P0A2D9; -.
DR SMR; P0A2D9; -.
DR STRING; 99287.STM4006; -.
DR PaxDb; P0A2D9; -.
DR EnsemblBacteria; AAL22845; AAL22845; STM4006.
DR GeneID; 1255532; -.
DR KEGG; stm:STM4006; -.
DR PATRIC; fig|99287.12.peg.4222; -.
DR HOGENOM; CLU_000445_114_39_6; -.
DR OMA; EIMLTTA; -.
DR PhylomeDB; P0A2D9; -.
DR BioCyc; SENT99287:STM4006-MON; -.
DR BRENDA; 2.7.13.3; 5542.
DR Proteomes; UP000001014; 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; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..349
FT /note="Sensory histidine kinase/phosphatase NtrB"
FT /id="PRO_0000074823"
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"
FT CONFLICT 177..178
FT /note="RL -> SV (in Ref. 1; CAA59424)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="D -> V (in Ref. 1; CAA59424)"
FT /evidence="ECO:0000305"
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
