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Database: UniProt
Entry: I9WJD9_9SPHN
LinkDB: I9WJD9_9SPHN
Original site: I9WJD9_9SPHN 
ID   I9WJD9_9SPHN            Unreviewed;       726 AA.
AC   I9WJD9;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=WSK_1131 {ECO:0000313|EMBL:EIZ80338.1};
OS   Novosphingobium sp. Rr 2-17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=555793 {ECO:0000313|EMBL:EIZ80338.1, ECO:0000313|Proteomes:UP000004732};
RN   [1] {ECO:0000313|EMBL:EIZ80338.1, ECO:0000313|Proteomes:UP000004732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RR2-17 {ECO:0000313|Proteomes:UP000004732};
RX   PubMed=22933764; DOI=10.1128/JB.01159-12;
RA   Gan H.M., Chew T.H., Hudson A.O., Savka M.A.;
RT   "Genome Sequence of Novosphingobium sp. Strain Rr 2-17, a Nopaline Crown
RT   Gall-Associated Bacterium Isolated from Vitis vinifera L. Grapevine.";
RL   J. Bacteriol. 194:5137-5138(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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EIZ80338.1}.
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DR   EMBL; AKFJ01000014; EIZ80338.1; -; Genomic_DNA.
DR   RefSeq; WP_008994084.1; NZ_AKFJ01000014.1.
DR   AlphaFoldDB; I9WJD9; -.
DR   PATRIC; fig|555793.3.peg.1134; -.
DR   eggNOG; COG5000; Bacteria.
DR   OrthoDB; 9776727at2; -.
DR   Proteomes; UP000004732; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
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; IPR017232; NtrY.
DR   InterPro; IPR045671; NtrY-like_N.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR44936:SF9; SENSOR HISTIDINE KINASE GLNK; 1.
DR   PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF19312; NtrY_N; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PIRSF; PIRSF037532; STHK_NtrY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EIZ80338.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004732};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        87..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          314..367
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          379..421
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          494..712
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   726 AA;  79884 MW;  FB1079E729B89DE5 CRC64;
     MQVAARRANF FAIIEVLSIL AFFIMTGATW IALNDGADKR ELLPSNLTAS LLVGTLVPAM
     AILVLLGRRM ALLRAAETSG GTGQMHVRLV FIFSLISAIP TLLVVIFASL LFQSGVEFWF
     SDSSRGLLEN ANKLARGFSE QTLRDVGYDS VALAEDSRTM LSAYPVASRE FQAFLADQVF
     RRKLDVAAII QIDANGQQRT PIILNPDGKS ENNRISPQDI ARLGKGEPYV ATAKDNRIIA
     SAPIDRESGV YALVVRKSDL FSLSQGERAQ NIVQAYEVLT NRARVYQLRF NVALFVLSLA
     LVGLSVWFAL RFADRQVKPL YELVDAARRV GAGNYALRIE GRTGADEIGL LNRAFNRMTA
     QIDKQTQALL GANRQLHERR LFIEAVLESV TSGIISLDEE GRVLLMNSTA QKLLGESTDD
     VPEGVLIQTL SPSIAAMLDQ GTVGGIVQYS RGGELLTLAV KTSRDATGHV ITFEDITRQL
     LDQRTAAWSD VARRIAHEIK NPLTPIQLAT ERLSRRYRKQ ITDNPELFDD LTRTIIRQVG
     DLRKMVDEFS SFARLPKPIF RAEDPISLTR QSLFLQEVAR PDIAFTFSSN NEPVTIACDR
     HQFGQAMTNV LKNAVEAIEA RAKEAPEDYK GAIGVEVIGG EGSIQVRITD NGIGLTQDRE
     RIIEPYVTTR EKGTGLGLAI VNKIVEEHGG EMTFTPADGG GTTVTMRFAE DPLAREEPGR
     KPEAAE
//
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