ID A0A158M7M1_9BORD Unreviewed; 435 AA.
AC A0A158M7M1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=phoR {ECO:0000313|EMBL:KAK96182.1};
GN ORFNames=L497_3513 {ECO:0000313|EMBL:KAK96182.1};
OS Bordetella holmesii CDC-H585-BH.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1331206 {ECO:0000313|EMBL:KAK96182.1, ECO:0000313|Proteomes:UP000026682};
RN [1] {ECO:0000313|EMBL:KAK96182.1, ECO:0000313|Proteomes:UP000026682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC-H585-BH {ECO:0000313|EMBL:KAK96182.1,
RC ECO:0000313|Proteomes:UP000026682};
RA Harvill E., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C., Cassiday P.,
RA Tondella M.L., Liao P., Zimmerman J., Meert K., Wessel D., Berger J.,
RA Dean J.M., Holubkov R., Burr J., Liu T., Brinkac L.M., Sanka R., Kim M.,
RA Losada L.;
RT "Genome sequence of Bordetella holmseii.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KAK96182.1}.
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DR EMBL; JFZZ01000044; KAK96182.1; -; Genomic_DNA.
DR RefSeq; WP_005018218.1; NZ_JFZZ01000044.1.
DR AlphaFoldDB; A0A158M7M1; -.
DR STRING; 35814.BBB42_02180; -.
DR GeneID; 56623422; -.
DR PATRIC; fig|1331206.3.peg.1149; -.
DR Proteomes; UP000026682; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:InterPro.
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 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; IPR021766; PhoR.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR014310; Sig_transdc_His_kinase_PhoR.
DR NCBIfam; TIGR02966; phoR_proteo; 1.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF11808; PhoR; 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 Kinase {ECO:0000313|EMBL:KAK96182.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:KAK96182.1}.
FT DOMAIN 210..428
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 435 AA; 48305 MW; 439C8FE6E5817DD0 CRC64;
MIWLRTLLLI VLWAVISLLL HALAGSPAGW VLFSAAMTAM VLWRSWRLQR VSAWAHDPDT
APPAGVGPWE DILAPLYRYT RARRRELAEL QDTMQGMLAA AQALPDGVVT LNEDYQIEWG
NRMARRHLGL RLPADRGQNL MNLLRSPEFV AYAHRSNWPE PILVRVGQSG QERVMMIQLA
TYASSRRLLI TRDVTQIEKL ETTRRDFVAN VSHELRTPLT VLAGFLETLH DMPPEALGEE
QRSQYLAMML EQAQRMQAIV EDLLTLSTLE SSPGTDPVAV NIQALLQTAR QQAEALSGGR
HHFEWQVDAN LDVLGSGSEL ASALSNLLTN AVRYTPEGGH ITVSWQGTPD GGARYSVRDT
GIGIPARHIP RLTERFYRVD RGRSRAVGGT GLGLAITKHI VLRHDAELLI ESEPGKGSTF
SLLFPPDRVV PAEPA
//
