ID   A0A7V9YJW3_9SPHN        Unreviewed;      1028 AA.
AC   A0A7V9YJW3;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   29-SEP-2021, entry version 2.
DE   RecName: Full=Histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HNQ29_000078 {ECO:0000313|EMBL:MBA2854094.1};
OS   Sphingobium sp. B10D3C.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=2735908 {ECO:0000313|EMBL:MBA2854094.1, ECO:0000313|Proteomes:UP000527231};
RN   [1] {ECO:0000313|EMBL:MBA2854094.1, ECO:0000313|Proteomes:UP000527231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B10D3C {ECO:0000313|EMBL:MBA2854094.1,
RC   ECO:0000313|Proteomes:UP000527231};
RA   Elkins J.;
RT   "Exploring microbial biodiversity for novel pathways involved in the
RT   catabolism of aromatic compounds derived from lignin.";
RL   Submitted (JUL-2020) 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};
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:MBA2854094.1}.
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DR   EMBL; JACDUG010000001; MBA2854094.1; -; Genomic_DNA.
DR   Proteomes; UP000527231; Unassembled WGS sequence.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 3.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 3.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 3.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          369..589
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          636..749
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          758..874
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          904..1026
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          594..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          269..362
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         685
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         807
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         959
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1028 AA;  111735 MW;  A3D1D124B376E9BD CRC64;
     MLHNNREVFL YAAIAFLLAI PFAGDLIFPL GTAVWVIYLL PTVLAFLASA PLAPLVTASL
     ATLLTIMGFF FARDGVDPNI AIVNRVIGAS VNWLLAAVGV MFIRSKLEIA RQDWLQAGQV
     GLGNAVAGDL SIEEVSQRAL RYLAEYLGAQ AAALFVREQA TFQRRAVYGV PQDAPIPLEI
     TPDDGLLGQA VRDKRSFLLT EVPENYLYYG SAFGRAVPQQ ILVAPARADG EVNAVIELGL
     TGKAAHDAEA FMTRIAAQLG VSIRSAAYRS QLQALLEETQ HQAEELQAQG EELQANNEEL
     EAQSQRLLES QARLEAQQAE LEESNASLEN QAHELEAQRD ELEQAQASLE EQTAELEKAS
     RYKSEFLANM SHELRTPLNS LLIMARLLGE NRAGNLSADQ VKHARTIESS GNDLLALIND
     ILDISKIEAG KVELDIRPAK LSTMFERLSA TFSAGATSKG LALRTEIDPG LPADIRTDAQ
     RVEQVLKNFL SNAIKFTAAG EITLRASAAP AGGVALSVRD TGIGIPAEKL GIIFDAFRQA
     DGTVSRKYGG TGLGLSISRE LAGLLGGSVG VESAAGEGSV FTLTLPLELE PSALDQGRSQ
     SRPALPEPAR GPAMPALPRQ SPVADDREVL SGDSRLILVV EDDARFAEIL ADLSHELGFQ
     CLVAGTADEG VLLARQYLPH AIILDMNLPD HTGLSVLDRL KRDVRTRHIP VHIVSVSEDA
     QAALANGAVG YLLKPVRREQ LVDMLEALET RISQRVRRVL VVEDDARQAE SIGLLLGSRD
     VETVAAHSAA ECLDRLGTTS FDCMVLDLNL PDTPGLDLLE RLSEDETIGF PPVIVYTGRD
     ISPEEELRLR RYSKSIIVKG AKSPERLLDE VTLFLHQVVS ELPEAQKEMV VRSLNRDVAL
     DGKTILVVED DIRNVYALTS IFEPHGTTIR IARNGREALD ALDQSAKGEA PMVDLVLMDV
     MMPEMDGLTA TRHIRGQSQW RNLPIIALTA KAMDRDQQEC LAAGANDYLS KPLDVDKLLS
     LVRVWMPR
//