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Database: UniProt
Entry: J2WK53_9SPHN
LinkDB: J2WK53_9SPHN
Original site: J2WK53_9SPHN 
ID   J2WK53_9SPHN            Unreviewed;       654 AA.
AC   J2WK53;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=PMI04_02367 {ECO:0000313|EMBL:EJK83035.1};
OS   Sphingobium sp. AP49.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK83035.1};
RN   [1] {ECO:0000313|EMBL:EJK83035.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP49 {ECO:0000313|EMBL:EJK83035.1};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJK83035.1}.
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DR   EMBL; AJVL01000057; EJK83035.1; -; Genomic_DNA.
DR   RefSeq; WP_007710116.1; NZ_CP124576.1.
DR   AlphaFoldDB; J2WK53; -.
DR   STRING; 1144307.PMI04_02367; -.
DR   PATRIC; fig|1144307.3.peg.2131; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   OrthoDB; 9796100at2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}.
FT   DOMAIN          9..66
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          84..136
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          137..194
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          212..264
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          284..504
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          527..636
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         576
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   654 AA;  71094 MW;  6F8EA57549E071B8 CRC64;
     MEIAETVESS NRFELLVQSI TDYAIFILDT RGLVASWNAG ARRFKGYEAH EIIGQHFSRF
     YTPEDQAAGI PALALHTAET EGRFEAEGWR VRKDGTCFWA NVVIDPIRDP AGVLIGFAKV
     TRDLTDRRAA QEELRRSEER FRMLVQSVTD YAIYMLDPVG TITSWNSGAE RFKGYRADEI
     LGQNFARFYS DEDRMAGLPS RALETAQREG RFEAEGWRIR KDGTRFWAGV VIDPIRSPSG
     TLVGFAKITR DLTERREATR ALDEAREAIF QSQKMDAIGK LTGGVAHDFN NLLAVIVGSL
     DLARQRLSTG ADITRYLDNA MTAAERGATL TQRMLAFARK QELQLRSVDC IGLVRDMADL
     LQTTLGTGIA IETRFPLTLR PAHADPAQLE LALINLAVNA RDAMAGSGKL IIEGSEIMLA
     ANEQPDLAAG GFVRLTVTDE GEGMDAPTLA RAREPFFTTK GIGKGTGLGL SMIHGFAQQC
     GGAMTISSVK GEGTSVSLWL PFAAAEAPAA PPPIASECHG SDLEHLVILA VDDDDLVLTN
     TAGMLEDLGH TVFLAGSATE ALAMLEQGHV DLVITDHAMP GMTGAQLADA IDEKHPGLPV
     IIVTGYAELP PQASHRLRLD KPFRQADLAG VLRRVRRDAP SGRLLQIGVD DGTD
//
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