ID A0A1V9ULG9_9PSED Unreviewed; 641 AA.
AC A0A1V9ULG9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BWR59_18690 {ECO:0000313|EMBL:OQR30569.1};
OS Pseudomonas sp. Bc-h.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1943632 {ECO:0000313|EMBL:OQR30569.1, ECO:0000313|Proteomes:UP000192462};
RN [1] {ECO:0000313|EMBL:OQR30569.1, ECO:0000313|Proteomes:UP000192462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bc-h {ECO:0000313|EMBL:OQR30569.1,
RC ECO:0000313|Proteomes:UP000192462};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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:OQR30569.1}.
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DR EMBL; MUIN01000009; OQR30569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9ULG9; -.
DR STRING; 1943632.BWR59_18690; -.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000192462; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR019247; Histidine_kinase_BarA_N.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF09984; sCache_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OQR30569.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 189..241
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 270..492
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 515..631
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 229..263
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 564
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 641 AA; 70968 MW; 6EC93D925B1A7958 CRC64;
MTAQRGWNIS TRTQILSLGP ALLLTLLLIS FFTVVRIQDL RQELTHTGQL IANQLAPASE
YGVIVGNNDV LESLMKATMS TPHVRFLEVQ DSTGQVLVHV EQAPENARDR QMEIFQAPIR
LQQVKGEGNR LDDADDIATA PIEDYLGRVL VGMSSDAFNL REQEILLKAG ILALFALLFT
YILARRLSLS LSQPISAMSD AVKAIQHGDY TAPLPVADDA ELGDLARHIN NLAQGLEKAS
REQKQAMDEL IRTREEAERA NSAKSEFLAM MSHELRTPMN GVLGMLQLME TTRMTEEQAE
YAALATESTE HLLRVINDIL DFSRFERDAL ELENISFNLA DLIATSVQAF AHNAQQRGLA
LELDLPQGLD QLQVKGDPTR IRQILVNLIG NALKFTEFGS VRVQPAWQQH DEQHILFSCA
VRDSGIGISP DLLESMFDAF QQADNSISRR YGGTGLGLPI ARNLAERMGG SLSAQSSEGL
GSVFNLQIPL QLIQQEEPQP QPGTVDEMRQ EREGCVLLVE DNPVNRTVVE AMLRSLGLQV
SAAGDGAEAV SMVSREKYAL ILMDCRLPVM DGYEATRRIR QLPGLETLPI IALTANARHG
DREICLQAGM NDYLAKPFKR TDLQQVLQRW LTFKPSATGD K
//
