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Database: UniProt
Entry: A0A023Y7L0_9GAMM
LinkDB: A0A023Y7L0_9GAMM
Original site: A0A023Y7L0_9GAMM 
ID   A0A023Y7L0_9GAMM        Unreviewed;       886 AA.
AC   A0A023Y7L0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DX03_18410 {ECO:0000313|EMBL:AHY60607.1};
OS   Stenotrophomonas rhizophila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=216778 {ECO:0000313|EMBL:AHY60607.1, ECO:0000313|Proteomes:UP000025222};
RN   [1] {ECO:0000313|EMBL:AHY60607.1, ECO:0000313|Proteomes:UP000025222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14405 {ECO:0000313|Proteomes:UP000025222};
RA   Alavi P., Starcher M.R., Thallinger G., Zachow C., Mueller H., Berg G.;
RT   "Is there a border between beneficial and pathogenic bacteria?";
RL   Submitted (APR-2014) 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; CP007597; AHY60607.1; -; Genomic_DNA.
DR   RefSeq; WP_038690969.1; NZ_CP007597.1.
DR   AlphaFoldDB; A0A023Y7L0; -.
DR   STRING; 216778.DX03_18410; -.
DR   GeneID; 61477886; -.
DR   HOGENOM; CLU_000445_113_2_6; -.
DR   Proteomes; UP000025222; 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, ECO:0000313|EMBL:AHY60607.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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        394..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        440..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        469..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          659..876
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   886 AA;  96744 MW;  31EA848D5FF60463 CRC64;
     MSDPRTRQAD ALVERLQREA GGKLTVFLGA APGVGKTFSM LSRAHEQLRR GVDVVVGLVE
     THGRAETSAL LEGLPQVPLL QRDYQQHVLG EMDLDAVLAR HPALVLVDEL AHRNVPGSRH
     ERRWQDVMEL LEAGIDVWTT VNIQHLESLN DVVMRITGVR VSETVPDAVL DRLHDIVLVD
     IPPRELIERL QQGKVYVPEQ AAQALQAFFS PANLTALREL AMQEAADRVD SSLRETRAAR
     GEGNLPLRRR VLVAIDGGGQ SEYLVRVGRR IAERRDAPWT VVTVQGRRND EATRREIDAA
     FALARRLGGE AELLHGSSIA DALLDHAAHN SVSTLILGRT RERPVARMLN RTLTQQLIQR
     GAHYEITIIG TPQARARARR TGLSVPSRST GQDTLLALGA TAIACLVALV AERWVGLYDL
     SMVFIVAVVM VAARSRTSAA VIAAALCFLA YNFFFIAPRF TFAISARQGV ITVFLFLAAA
     LVAGRLASRL RMQVLALRAA NRHANARQAL GRQLTRAASN EEVAQAGREA LEQAMDAPAW
     LRIGQDTSTS GSAAPGDTDL AAADWARRHG QPSGRFTDTL AGAEWWFLPL LDGDDRAIGV
     AGMRFARNAP RLTPEQRQLA EAMVDDIAQA ALRTQLVADL EKAHVSNETE RLRSALLSSV
     SHDLRSPLAA MIGSADSLGS YADAMDAQDR RALLDTILVE GERLDRYIQN LLDMTRLGHE
     GLQINRDWIG VDELVGSAAR RLQRYQPEVQ LKLDIPATLA PIWVHPALVE QAVFNVMENA
     AKFSPPGAAV EVQARLVEGE LRIDVLDAGP GIPDDERARI FDMFYSVERG DRGRHGTGLG
     LTICQGMIGA HGGSVQALPG RDGRGTLIRI TLPLLQPHPA DDHDDP
//
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