DCTB_PSEAE
ID DCTB_PSEAE Reviewed; 612 AA.
AC Q9HU20;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=C4-dicarboxylate transport sensor protein DctB {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P13633};
GN Name=dctB {ECO:0000303|PubMed:21725012};
GN OrderedLocusNames=PA5165 {ECO:0000312|EMBL:AAG08550.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=21725012; DOI=10.1128/jb.05074-11;
RA Valentini M., Storelli N., Lapouge K.;
RT "Identification of C(4)-dicarboxylate transport systems in Pseudomonas
RT aeruginosa PAO1.";
RL J. Bacteriol. 193:4307-4316(2011).
CC -!- FUNCTION: Member of the two-component regulatory system DctB/DctD,
CC which regulates C4-dicarboxylate transport via regulation of expression
CC of the dctPQM operon and dctA (PubMed:21725012). DctB functions as a
CC membrane-associated protein kinase that phosphorylates DctD in response
CC to environmental signals (By similarity).
CC {ECO:0000250|UniProtKB:P13633, ECO:0000269|PubMed:21725012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P13633};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P13633}.
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DR EMBL; AE004091; AAG08550.1; -; Genomic_DNA.
DR PIR; F83000; F83000.
DR RefSeq; NP_253852.1; NC_002516.2.
DR RefSeq; WP_003123664.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HU20; -.
DR SMR; Q9HU20; -.
DR STRING; 287.DR97_2533; -.
DR PaxDb; Q9HU20; -.
DR PRIDE; Q9HU20; -.
DR EnsemblBacteria; AAG08550; AAG08550; PA5165.
DR GeneID; 879962; -.
DR KEGG; pae:PA5165; -.
DR PATRIC; fig|208964.12.peg.5413; -.
DR PseudoCAP; PA5165; -.
DR HOGENOM; CLU_000445_94_2_6; -.
DR InParanoid; Q9HU20; -.
DR OMA; WRFRATR; -.
DR PhylomeDB; Q9HU20; -.
DR BioCyc; PAER208964:G1FZ6-5282-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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:0032892; P:positive regulation of organic acid transport; IMP:PseudoCAP.
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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Coiled coil; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..612
FT /note="C4-dicarboxylate transport sensor protein DctB"
FT /id="PRO_0000435376"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 385..599
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT COILED 328..376
FT /evidence="ECO:0000255"
FT MOD_RES 388
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 612 AA; 68533 MW; A2D0988C6632A583 CRC64;
MPRILAATAG SFVLKAYFHR WRSLVILALL LAPLLWPLQY FAERYYSEQL AEQNRQTLDL
YVANLLGTLR RYEELPQILG GLPVLRQALQ QPGDPLLQKI ANEALADIRR RTGADVIYLL
QPDGTTQVAS NWAQADSFVH RNFAFRPYYR EAMQGRLARF FGLGTTSIKR GYYFASAVKE
GSRIIGVLVV KVDLEHIERL WGNSPEQLLV IDNYGVVILS SREDWRFHAS RPLSAAERDE
IHANIPYPVQ DPKPLRLQQS AWLSQSRTLP ETGWTVSIYA PRTLIERPVR SVLLIGGATL
LALLLLLTLL TLSRRHYLDR IALEAEAKRQ LEERVLERTR ELENANAQLQ QEVHEREQAQ
RELMRAQDEV VQAGKLTALG TMSASISHEL NQPLAAIRSY ADNARVLLDH QRTEDARGNL
EQISDLTTRM ASIIAHLKAY ARGARRAPEN VQLQPAIEDA LSMVASRRRA MNVELLRDVP
DAPLWVQAGE TRLRQILGNL LTNALDALAE KAPPRRLWVI ASQDQHGVTL TLRDNGPGFS
EDALAHAHEP FFTTKTTAKG LGLGLAICDN LLRALGGRLE MGNHLEGGAV VRLHLLPGVP
GVAAMPQEET RA
