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Database: UniProt
Entry: A0A031J9Q0_9SPHN
LinkDB: A0A031J9Q0_9SPHN
Original site: A0A031J9Q0_9SPHN 
ID   A0A031J9Q0_9SPHN        Unreviewed;       976 AA.
AC   A0A031J9Q0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, 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=BES08_22600 {ECO:0000313|EMBL:AOR79588.1}, BV97_05335
GN   {ECO:0000313|EMBL:EZP70889.1};
OS   Novosphingobium resinovorum.
OG   Plasmid pSA1 {ECO:0000313|EMBL:AOR79588.1,
OG   ECO:0000313|Proteomes:UP000094626}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=158500 {ECO:0000313|EMBL:EZP70889.1, ECO:0000313|Proteomes:UP000024329};
RN   [1] {ECO:0000313|EMBL:EZP70889.1, ECO:0000313|Proteomes:UP000024329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KF1 {ECO:0000313|EMBL:EZP70889.1,
RC   ECO:0000313|Proteomes:UP000024329};
RA   Gan H.M., Gan H.Y., Chew T.H., Savka M.A.;
RT   "Whole genome sequence of Novosphingobium resinovorum KF1.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOR79588.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA1 {ECO:0000313|EMBL:AOR79588.1};
RC   PLASMID=pSA1 {ECO:0000313|EMBL:AOR79588.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000094626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA1 {ECO:0000313|Proteomes:UP000094626};
RX   PubMed=27851894; DOI=10.1016/j.jbiotec.2016.11.013;
RA   Hegedus B., Kos P.B., Balint B., Maroti G., Gan H.M., Perei K., Rakhely G.;
RT   "Complete genome sequence of Novosphingobium resinovorum SA1, a versatile
RT   xenobiotic-degrading bacterium capable of utilizing sulfanilic acid.";
RL   J. Biotechnol. 241:76-80(2017).
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; CP017076; AOR79588.1; -; Genomic_DNA.
DR   EMBL; JFYZ01000064; EZP70889.1; -; Genomic_DNA.
DR   RefSeq; WP_008830371.1; NZ_JFYZ01000064.1.
DR   AlphaFoldDB; A0A031J9Q0; -.
DR   KEGG; nre:BES08_22600; -.
DR   PATRIC; fig|158500.4.peg.5407; -.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   OrthoDB; 9796100at2; -.
DR   Proteomes; UP000024329; Unassembled WGS sequence.
DR   Proteomes; UP000094626; Plasmid pSA1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd18161; REC_hyHK_blue-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 2.
DR   Gene3D; 3.30.450.40; -; 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; 3.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
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; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 3.
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; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EZP70889.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:AOR79588.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          389..441
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          442..514
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          518..570
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          608..832
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          859..975
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          561..592
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         909
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   976 AA;  108237 MW;  0C613488D2FDAD76 CRC64;
     MTDAFGRPSH EELRKWQAFQ LRLLDRMRRS EDAEDILATA AQLLGEHLSA GRCGFATISD
     DGVRAHLDAD WSSTLPSLAG ETRVLDSFGP AIIAELRLGH TLVVADSDTD PRTAAFAEGW
     RSIGSHALVV CPIFREGRFD SVLYVHHATP RIWTESETRQ VEDVALRTRD AVDRARSEVA
     LRASEQRYRS LFNSIDSGFC VVEVVFDDDG KASDYRFIEV NDSFEAYTGI ANAQGRWMRE
     IAPAHEQHWF DLYGRVARTG RPERIELPAR QLDDRWYAVQ AYRVDDPARH HVAVLFTDLT
     ARRRTERALE RSREELELAV RAAELGRFDY RPREGTLTWD DRCRALFGLS PGVSVSYETA
     FLAGLHPEDR DRADRAVAAS LDPDGSHHFE VEYRTIGIED GELRHISAHG LAFFEGRAPV
     RLIGTVQDVT SDREANAALR EVGERLRLAG RATNDAVWDW DLRADHVTWN EALAHAYGHV
     PEAVAPTGEW WLSQIHPDDA RRIHESIFRV IDGQGTDWTD EYRFRRADGS YADVLDRGYV
     IRDEAGRPQR MVGAMQDVSA RKAVERQLEE ERRRLHEEVL ETAAERDRAE DALRQSQKME
     AVGQLTGGLA HDFNNLLAGI SGALEMIHTR IGQGRTGELE KYSTAAQGAV RRAAALTHRL
     LAFSRRQTLA PTPTDVAALV VGIEDLVRRT VGPQVEVRTS SSSGLWSTLV DPNQLENALL
     NLCINARDAM PGGGIIRISS ANVTLSDRQA REQDLEPGEY VEISVSDTGT GMTPAVVERA
     FDPFFTTKPI GEGTGLGLSM IYGFARQSGG QIGIATQPGQ GTIMRLYLPR HEGTEAPAAV
     AAPVPEQEPV AERSQRTGRI LVVDDEPTVR MLVVEVVEEL GYRVMKAHDG PSAMRIIESG
     QPIDLLITDV GLPGGMNGRQ IADAALARLP ALKVLFITGY AEQTVMSNNQ LAPNMAIMTK
     PFAMEALANR IREIAD
//
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