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Database: UniProt
Entry: B2I9R3_XYLF2
LinkDB: B2I9R3_XYLF2
Original site: B2I9R3_XYLF2 
ID   B2I9R3_XYLF2            Unreviewed;       555 AA.
AC   B2I9R3;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=XfasM23_2036 {ECO:0000313|EMBL:ACB93434.1};
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441 {ECO:0000313|EMBL:ACB93434.1, ECO:0000313|Proteomes:UP000001698};
RN   [1] {ECO:0000313|EMBL:ACB93434.1, ECO:0000313|Proteomes:UP000001698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23 {ECO:0000313|EMBL:ACB93434.1,
RC   ECO:0000313|Proteomes:UP000001698};
RX   PubMed=20601474; DOI=10.1128/JB.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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; CP001011; ACB93434.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2I9R3; -.
DR   KEGG; xfn:XfasM23_2036; -.
DR   HOGENOM; CLU_000445_114_39_6; -.
DR   Proteomes; UP000001698; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ACB93434.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:ACB93434.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        72..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        122..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          340..550
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   555 AA;  61088 MW;  48B86C4BE3DBA559 CRC64;
     MSPVVSILGY LSSALGHRDV LFSASLIHRI EFAPQRELYF LALYRILEAG LIAALVFSPV
     SLLVDPESDP HLGTVVAVGY LLLATILLVW GRNERWFTPL VFGSTVADIL AATLAIHALP
     KASAGIAMML LFNVAAAAIL LRLRFSMILA WIAGVAMLVE YIWTVLSEGD SSRSLAELLM
     FFTSYTAVAY MCHQAAQRAR YSQALAEKRR AQIVNLAEIN ELIIRRMRTG VLVVDAANRI
     GLSNETAAAL LGYDRQLVES DYDLATVAPE LIMRLKCWRI GRHYEDTPLR LAPDQPEVQP
     RFVSLLADSG LTLIFLDDVS VVSRRAESLT LLALGRFSAS LAHEIRNPLA AIKHASQLLE
     ESSNLDKGDQ RLLDIILKQC QRTNGIVESV LGLARRERAN PENLDLVGFV SRFVDEYRQT
     LSSEYDNLEI QTLHSTVQAL VDPRHLYQIL AVLTHNALRY GRFPDTPAQV RIEVVYTGGS
     VGINVLDQGP GIPDAAVLQL FQPFFTTSDH GTGLGLYIAR ELCNANQSNL EYVAIPGGGA
     CFRITLPGPY ALIPN
//
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