ID A0A261TEU7_9BORD Unreviewed; 353 AA.
AC A0A261TEU7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ORFNames=CAL25_16010 {ECO:0000313|EMBL:OZI48164.1};
OS Bordetella genomosp. 5.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1395608 {ECO:0000313|EMBL:OZI48164.1, ECO:0000313|Proteomes:UP000216913};
RN [1] {ECO:0000313|EMBL:OZI48164.1, ECO:0000313|Proteomes:UP000216913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU10456 {ECO:0000313|EMBL:OZI48164.1,
RC ECO:0000313|Proteomes:UP000216913};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZI48164.1}.
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DR EMBL; NEVP01000010; OZI48164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261TEU7; -.
DR Proteomes; UP000216913; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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; 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; PF13426; PAS_9; 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.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000313|EMBL:OZI48164.1};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000216913};
KW Transferase {ECO:0000313|EMBL:OZI48164.1}.
FT DOMAIN 1..54
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 131..351
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 353 AA; 39038 MW; 44A19DBD094D22D8 CRC64;
MNVDAFDFLA TSVFLLNERG HIEYANAASE DLFGRSRKQL RGASAATLFD HPEDLQTSID
GAVAGKFADV RQLSSFRRGS ESAEVTVTTV ALTGQTWPVL IETREIEQRV LADRNHRLVD
EIESHRELLR NLAHEVKNPL GGLRGAAQLL EAELPSAELA EYTQVIISEA DRLQALVDRL
SGPQRVPLNT RPVNIHEICE RVCALIQAEF RDSVTLVRDY DASVPDIPGD AARLMQAVLN
VARNAAQELN LQKGSDVPPG QIVLRTRVAR QVMLAHRHHR LALVLSIIDN GPGVPEHIRD
RIFHPLVTAR AGGTGLGLSL SQDFVQQHGG IIEFESRPRH TEFRLVLPME SSL
//
