ID A0A2V4Z9K3_9RHIZ Unreviewed; 608 AA. AC A0A2V4Z9K3; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 12-AUG-2020, entry version 10. DE RecName: Full=C4-dicarboxylate transport sensor protein {ECO:0000256|PIRNR:PIRNR036431}; DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR036431}; GN ORFNames=C7491_106153 {ECO:0000313|EMBL:PYF57253.1}; OS Ensifer sp. AP48. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae; OC Sinorhizobium/Ensifer group; Ensifer; unclassified Ensifer. OX NCBI_TaxID=2135475 {ECO:0000313|EMBL:PYF57253.1, ECO:0000313|Proteomes:UP000247575}; RN [1] {ECO:0000313|EMBL:PYF57253.1, ECO:0000313|Proteomes:UP000247575} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP48 {ECO:0000313|EMBL:PYF57253.1, RC ECO:0000313|Proteomes:UP000247575}; RA Pelletier D.; RT "Populus root and rhizosphere microbial communities from Tennessee, USA."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Member of the two-component regulatory system DctB/DctD CC involved in the transport of C4-dicarboxylates. DctB functions as a CC membrane-associated protein kinase that phosphorylates DctD in response CC to environmental signals. {ECO:0000256|PIRNR:PIRNR036431}. 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 ECO:0000256|PIRNR:PIRNR036431}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|PIRNR:PIRNR036431}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PIRNR:PIRNR036431}. 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:PYF57253.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QKLQ01000006; PYF57253.1; -; Genomic_DNA. DR Proteomes; UP000247575; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule. DR CDD; cd00082; HisKA; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR033479; dCache_1. 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; IPR029151; Sensor-like_sf. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR InterPro; IPR017055; Sig_transdc_His_kinase_DctB. DR Pfam; PF02743; dCache_1; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PIRSF; PIRSF036431; STHK_DctB; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF103190; SSF103190; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|PIRNR:PIRNR036431}; KW Cell inner membrane {ECO:0000256|PIRNR:PIRNR036431}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, KW ECO:0000256|PIRNR:PIRNR036431}; Coiled coil {ECO:0000256|SAM:Coils}; KW Kinase {ECO:0000256|PIRNR:PIRNR036431, ECO:0000313|EMBL:PYF57253.1}; KW Membrane {ECO:0000256|PIRNR:PIRNR036431}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR036431}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transferase {ECO:0000256|PIRNR:PIRNR036431}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|PIRNR:PIRNR036431}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|PIRNR:PIRNR036431}; KW Two-component regulatory system {ECO:0000256|PIRNR:PIRNR036431}. FT TRANSMEM 291..313 FT /note="Helical" FT /evidence="ECO:0000256|PIRNR:PIRNR036431" FT DOMAIN 387..600 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT COILED 344..371 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 608 AA; 66685 MW; 25A1681B8F45294A CRC64; MKFRLALGFL LLPLLATMLA WKGYAVTTDS YLREATAQAT TALRLAVTAL DGHLNRYQAL PALIADHEDV QELVTRPRDR RLREAVNTYL KDINALLHSS DIYVITPDGE TIAASNYDGP TSFVGQNFSY RPYFQEALRG QQSRFYALGT TSLKRGYYFG SPIQIGDEIR GVIVFKVDVE SIEASWQGGE YRIFVSDPEG IIFMSGDPDW LYSSILPLTS DRLARTEASR RYADATLRPL PMGESNASDH RFMTVSSGGS SREYLVLSQY MPDADWTVNV LVDTASAYTQ ALTTVAAALL LICLAGLGVA IILQRRARLN ERISMQAEAQ VELARRVDER TADLARVNTQ IEEEIAERRL TEQQLRRTQA DLIQAGKLAG LGQMSAALSH EFNQPLAAAK TYADSAALLI ERGRSDEATD NIRRISGLVD RMAAISKHLR NFARKPNEKL GPVPVEEAVR DTLEIVSVRL KAAAATIDID LGNKPLVVRA GSVRLQQVLV NIISNAADAV EGLDDRTIRL RARQEDHKVV LTVSDRGPGI APAIAERIFD PFFSTKGVGK GLGLGLSISY NIIKDFGGSL IATNLAEGGA EFRIELAAEN SNAREAAE //