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Database: UniProt
Entry: D2UFZ5_XANAP
LinkDB: D2UFZ5_XANAP
Original site: D2UFZ5_XANAP 
ID   D2UFZ5_XANAP            Unreviewed;       892 AA.
AC   D2UFZ5;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=KdpD {ECO:0000313|EMBL:CBA17306.1};
GN   OrderedLocusNames=XALc_2829 {ECO:0000313|EMBL:CBA17306.1};
OS   Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA17306.1, ECO:0000313|Proteomes:UP000001890};
RN   [1] {ECO:0000313|EMBL:CBA17306.1, ECO:0000313|Proteomes:UP000001890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX   PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA   Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA   Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA   Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA   Rott P.;
RT   "The complete genome sequence of Xanthomonas albilineans provides new
RT   insights into the reductive genome evolution of the xylem-limited
RT   Xanthomonadaceae.";
RL   BMC Genomics 10:616-616(2009).
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; FP565176; CBA17306.1; -; Genomic_DNA.
DR   RefSeq; WP_012917299.1; NC_013722.1.
DR   AlphaFoldDB; D2UFZ5; -.
DR   STRING; 380358.XALC_2829; -.
DR   GeneID; 57878136; -.
DR   KEGG; xal:XALC_2829; -.
DR   PATRIC; fig|29447.3.peg.2787; -.
DR   eggNOG; COG2205; Bacteria.
DR   OrthoDB; 9806130at2; -.
DR   Proteomes; UP000001890; Chromosome.
DR   GO; GO:0016020; C: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; cd01987; USP_OKCHK; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR   InterPro; IPR006016; UspA.
DR   PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR   PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR   Pfam; PF13493; DUF4118; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF02702; KdpD; 1.
DR   Pfam; PF00582; Usp; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001890};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        395..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        424..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        470..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          664..881
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   892 AA;  97810 MW;  65DE78713F8BC5F3 CRC64;
     MSDLRTQQAD ALIGELKRER GGRLTVFLGA APGVGKTYAM LSRARQLQQQ GSVLVIGVVE
     THGRVETAAL LEGLTVQPRR RVEYRGRTLD EMDLDALLAL RPPLVLVDEL AHRNAPGSRH
     ERRWQDVEEL LDAGIDVYST VNIQHLESLN DVVHRITGVR VSETVPDAMF DRLRDIVLVD
     LPPRELIERL QQGKVYLPEQ AGQALQAFFS PSNLAALREL AMQTAADRVD NDLRDVQAAQ
     GRPGLALRRR VMVAIDGRGQ SDYLVRVARR VAERRGSPWT VVTVQTQAQP EEAWQLEIDR
     AFALARRLGG DAALLRGSSV ADALLDHAAR NGVSTLLLGR TRERPLARMI NRTLTQQLLQ
     RGAHYELVII SSPEARARSR RRWRSPGHWL SRDDLAFAMV ASALAVVVAW IAERWVGIDD
     LSMVFIVAVV MVAAKTRMAA AVLAALLSFF GYNFFFIEPR FTFQIGTRQG VVTVLLFLVA
     ALVAGRLASR LRSQVLALRA ANAQTTALQR LGRELTSAAD LGQVLDAGRH ALSTTLDAEA
     WVRLQPLEAA HAGADDYAPS MAAVDRSAAD WAQRHGQATG RFTDTLAGAS WWFLPVRHER
     GAIGVVGLRF AAGVQRPGLE QQRLAEAMVE DIGQAALRTR LVADLESARV SGETEHLRSA
     LLSSVSHDLR SPLAAMIGAA SSLSSYGQAM SAEDRRSLLD TIQMEGERLD RYIQNLLDMT
     RLGHNGLTLN RDWIGVDELI GSAARRLQRY QPEVLLDIVL AADLPTLWVH PALVEQAVFN
     VLENAAKFSP PDTAIRVAAM MVEGRLRIDI ADRGPGIPED ERARIFDMFY SVERGDRGRH
     GTGLGLTICQ GMIGAHGGSV EALPGPDGRG TTIRITLPLI EPAAPPRRPD AD
//
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