ID   A0A1I0NW84_9GAMM        Unreviewed;       644 AA.
AC   A0A1I0NW84;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04515660_2200 {ECO:0000313|EMBL:SEW06101.1};
OS   Luteibacter sp. 329MFSha.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1798239 {ECO:0000313|EMBL:SEW06101.1, ECO:0000313|Proteomes:UP000199162};
RN   [1] {ECO:0000313|EMBL:SEW06101.1, ECO:0000313|Proteomes:UP000199162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=329MFSha {ECO:0000313|EMBL:SEW06101.1,
RC   ECO:0000313|Proteomes:UP000199162};
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};
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DR   EMBL; FOJE01000001; SEW06101.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0NW84; -.
DR   STRING; 1798239.SAMN04515660_2200; -.
DR   Proteomes; UP000199162; Unassembled WGS sequence.
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; 3.40.50.2300; -; 2.
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; IPR011006; CheY-like_superfamily.
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; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
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; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}.
FT   DOMAIN          6..123
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          288..508
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          528..643
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          235..281
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         55
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         578
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   644 AA;  70533 MW;  45676BE3A0CBDCDE CRC64;
     MPRNSRLLIV DDNAATRYAM RRTVERAGYE AMEAGTGTEG LALLASHEFA AVILDVNLPD
     MSGFDIVRRL REAPETMLLP VVHVSAASID TGDLITGLDN GADAYLIHPV DPDVMLATLR
     TLMRVRETED ELRAAEARFR EIFTNIAAPI AVVDGALRIL DSNEAFDRLI EDAGCTGELV
     SCFEPGQDET LAQMREHLAS NERWRGVLCM HSRAGVRETE WRVTPYRKEG GLVFVEDVTE
     QRRRERDQLE RIDTAHSQLA IEKAERERTE LQLLQAQKMD ALGKLTGGIA HDFNNLLTSI
     ITGIDLINRQ VEAGKPDKVQ RFADAVLGSA RRAAALTHRL LAFARQQPLD AKASDLKGNV
     RSLEDMLRRT LGERVTLELD LSGEPVVAEV DTNQLENAVI NLVINARDAM PEGGRIRIAT
     GRRRLVGDGS LPDGDYVHVT VSDNGSGIAP DVLQKVFEPF FTTKPLGQGT GLGLSMIYGF
     ARQSGGEARI ESVVGRGTEV TLLLPASEGE VVTVTAGQGE IAGGHGERVL LVEDTDSLRM
     FTAEVLTQAG YTCVATGDTD RALSLLRGDE SFDLLLTDIG MPGLDGRELA DVARAWRPTL
     PVLFMTGYAE NATERSRFLN RGMDLIAKPF EIDALLTRVR QMLD
//