ID A0A1H1DFV4_9GAMM Unreviewed; 877 AA.
AC A0A1H1DFV4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216569_1920 {ECO:0000313|EMBL:SDQ75415.1};
OS Pseudoxanthomonas sp. CF125.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1855303 {ECO:0000313|EMBL:SDQ75415.1, ECO:0000313|Proteomes:UP000199049};
RN [1] {ECO:0000313|EMBL:SDQ75415.1, ECO:0000313|Proteomes:UP000199049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF125 {ECO:0000313|EMBL:SDQ75415.1,
RC ECO:0000313|Proteomes:UP000199049};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FNLD01000002; SDQ75415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1DFV4; -.
DR STRING; 1855303.SAMN05216569_1920; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000199049; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.250.3020; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_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; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; NF041832; near_NosP_CTERM; 1.
DR PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SDQ75415.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199049};
KW Transferase {ECO:0000313|EMBL:SDQ75415.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 523..735
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 759..874
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 28..62
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 809
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 877 AA; 97089 MW; 1437AF3DF52120B8 CRC64;
MVPSVRPRLR LLLAGLAIAL AIGLLSALAA WQAEQRSLRA SAEQAREQLR LHRDTLDAIV
ERYRMLPAVL ALDPEVRDAL AGDTRDAAVV ERLNRKLEQV NGVATTSTLT LLDRNGKAIA
ASNWRTPNSN VGTDYGFRPY FQQAMADGTG DFYALGYTTG VPGYFLSQAV RDAQGRALGV
LVVKLVFNEL EAAWRTLPDP VFVSDAHGVI FLSGRDRWRY LDLRPLRESE RSELARTRQY
GEVPQRLLQY RELQAFAPGV RRVRLPGQGE HIWLSQALPE QGWTLHLLHS TRSSAAAART
VAIAVAGGLL AAAFLWLSVH QRRRLARLRE RSRVELQQLV EQHAIELRTA QDGLVQAAGG
ADYGESPSLQ HLPQGVCVID ADLRLVAWNR RYIELFKFPA GFIHVGLPIE EVFRYNARRG
LLGPGPIEEA IARRLDHLRS GKPHMHERER SDGTVIEIRG NPLPDGGFVT SYADITAYKQ
AARDLRSLAD ALEHRIGERT RDLAVAKSEA ENANRSKTRF VAAAVHDLLQ PLNAARMFVS
AMRDKLQEPQ ARQLADNVED ALAAQDAILN SLLDISRLES GALETRVRDF PLAPLLETLA
REFGMLAHAR GLRLDWVRTQ AVVRSDEALL RRILQNFLSN ALRYTPKGRI LLGCRRVEGG
LRIEVHDTGP GIPEARQQEI FEEFRRLDDG AGDDRGAGLG LAIVERIARL LGHRVDLRSS
VGRGSCFSVL VPLGDSGAVA APVIEAAAAD DDQELRDCMV WCVDDDPRVC EASRALLQRW
SCRVELAAGA GEALAAARPG AAPRLLLLDM RLGDTTGPEL YPQLVERWGS EPIVILVTAE
QDDTVRAIAR QHDWGYLPKP VRPAALRALI TQMLLRQ
//