NTRB_SHIFL
ID NTRB_SHIFL Reviewed; 349 AA.
AC P0AFB7; P06712;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=SF3939, S3807;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN45374.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18824.1; -; Genomic_DNA.
DR RefSeq; NP_709667.1; NC_004337.2.
DR RefSeq; WP_000190577.1; NZ_WPGW01000069.1.
DR AlphaFoldDB; P0AFB7; -.
DR SMR; P0AFB7; -.
DR STRING; 198214.SF3939; -.
DR EnsemblBacteria; AAN45374; AAN45374; SF3939.
DR EnsemblBacteria; AAP18824; AAP18824; S3807.
DR GeneID; 1026507; -.
DR GeneID; 60902695; -.
DR GeneID; 66672225; -.
DR KEGG; sfl:SF3939; -.
DR KEGG; sfx:S3807; -.
DR PATRIC; fig|198214.7.peg.4643; -.
DR HOGENOM; CLU_000445_114_39_6; -.
DR OMA; EIMLTTA; -.
DR OrthoDB; 1755994at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000074824"
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
