ID A0A1R4GNK8_9GAMM Unreviewed; 414 AA.
AC A0A1R4GNK8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:SJM69704.1};
GN ORFNames=A1232T_00820 {ECO:0000313|EMBL:SJM69704.1};
OS Psychrobacter piechaudii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1945521 {ECO:0000313|EMBL:SJM69704.1, ECO:0000313|Proteomes:UP000188357};
RN [1] {ECO:0000313|EMBL:SJM69704.1, ECO:0000313|Proteomes:UP000188357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Psychrobacter_piechaudii {ECO:0000313|EMBL:SJM69704.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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; FUGE01000100; SJM69704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4GNK8; -.
DR STRING; 1945521.A1232T_00820; -.
DR OrthoDB; 9789238at2; -.
DR Proteomes; UP000188357; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 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; IPR035965; PAS-like_dom_sf.
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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000188357};
KW Transferase {ECO:0000313|EMBL:SJM69704.1}.
FT DOMAIN 171..408
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 414 AA; 46790 MW; B42923B228D86E14 CRC64;
MKPLQALSLL QNLYTGVIWV AEDLTIQWVN SQTEQLLLVS KSRLIGLSIL DLLIPTMSET
KVITAESESL NQSTDPKAQL SENKSCVEAS RDKLELQFHN AKEYLQPFIE YSRHIRGVNQ
PLHVHYSVTP MNQESGSYYL IEIWQGDRQS RLDKEQRLQE QHDVSREMLR SVAHEVKNPL
AGIRGAAQLL IQQTQHPSEA TNNGENTVLV DAKKLTTYAG IVISETDRLT KLIEQLLGSN
QLPEWQSVNI HEPLEHVLLL IQSQYPQVTI KRDYDLSLPE ITADKNQLIQ VFLNLVNNAC
EALSEQDTTL LQAEYQPQLT LITRIEHQYT IGAQHHRQVI RVSIQDNGAG IADDLIERIF
FPLVTGRANG TGLGLALVQE IIHRHEGAIE VSSQPGDTHF NVYLPLQLSN LHPQ
//
