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Database: UniProt
Entry: E0J4T9_ECOLW
LinkDB: E0J4T9_ECOLW
Original site: E0J4T9_ECOLW 
ID   E0J4T9_ECOLW            Unreviewed;       349 AA.
AC   E0J4T9;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Sensory histidine kinase/phosphatase NtrB {ECO:0000256|ARBA:ARBA00039567};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   AltName: Full=Nitrogen regulation protein NR(II) {ECO:0000256|ARBA:ARBA00042313};
DE   AltName: Full=Nitrogen regulator II {ECO:0000256|ARBA:ARBA00043094};
GN   Name=glnL {ECO:0000313|EMBL:ADT77482.1};
GN   OrderedLocusNames=ECW_m4172 {ECO:0000313|EMBL:ADT77482.1};
OS   Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC
OS   13500 / NCIMB 8666 / NRRL B-766 / W).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=566546 {ECO:0000313|EMBL:ADT77482.1, ECO:0000313|Proteomes:UP000008525};
RN   [1] {ECO:0000313|EMBL:ADT77482.1, ECO:0000313|Proteomes:UP000008525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 /
RC   NCIMB 8666 / NRRL B-766 / W {ECO:0000313|Proteomes:UP000008525};
RX   PubMed=21208457; DOI=10.1186/1471-2164-12-9;
RA   Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y.,
RA   Nielsen L.K.;
RT   "The genome sequence of E. coli W (ATCC 9637): comparative genome analysis
RT   and an improved genome-scale reconstruction of E. coli.";
RL   BMC Genomics 12:9-9(2011).
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:0000256|ARBA:ARBA00037696}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; CP002185; ADT77482.1; -; Genomic_DNA.
DR   RefSeq; WP_000190577.1; NZ_WBMH01000024.1.
DR   AlphaFoldDB; E0J4T9; -.
DR   SMR; E0J4T9; -.
DR   GeneID; 83578595; -.
DR   KEGG; elw:ECW_m4172; -.
DR   PATRIC; fig|566546.30.peg.4232; -.
DR   Proteomes; UP000008525; Chromosome.
DR   GO; GO:0005524; F:ATP binding; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd16918; HATPase_Glnl-NtrB-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 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   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF16; SENSORY HISTIDINE KINASE_PHOSPHATASE NTRB; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          5..59
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          136..349
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
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
//
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