DCTA2_PSEAE
ID DCTA2_PSEAE Reviewed; 436 AA.
AC Q9I4F5;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=C4-dicarboxylate transport protein 2 {ECO:0000305};
GN Name=dctA2; Synonyms=dctA {ECO:0000303|PubMed:21725012};
GN OrderedLocusNames=PA1183;
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, INDUCTION, AND DISRUPTION PHENOTYPE.
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: Responsible for the transport of dicarboxylates such as
CC succinate, fumarate, and malate from the periplasm across the inner
CC membrane. {ECO:0000255|HAMAP-Rule:MF_01300,
CC ECO:0000269|PubMed:21725012}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01300}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01300}.
CC -!- INDUCTION: Expression is maximal in early exponential growth phase and
CC declines with cell density to reach a plateau in the stationary growth
CC phase. Induced by the C(4)-dicarboxylates succinate, fumarate and
CC malate. Positively regulated by RpoN and the DctB/DctD two-component
CC system. Negatively autoregulated. {ECO:0000269|PubMed:21725012}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene causes a growth defect
CC in minimal media supplemented with succinate, fumarate or malate. The
CC dctA-dctPQM double mutant shows no growth on malate and fumarate and
CC residual growth on succinate. {ECO:0000269|PubMed:21725012}.
CC -!- MISCELLANEOUS: The DctPQM carrier is more efficient than the DctA
CC carrier for the utilization of succinate at micromolar concentrations,
CC whereas DctA is the major transporter at millimolar concentrations.
CC {ECO:0000269|PubMed:21725012}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000255|HAMAP-Rule:MF_01300}.
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DR EMBL; AE004091; AAG04572.1; -; Genomic_DNA.
DR PIR; D83498; D83498.
DR RefSeq; NP_249874.1; NC_002516.2.
DR RefSeq; WP_003082442.1; NZ_QZGE01000006.1.
DR AlphaFoldDB; Q9I4F5; -.
DR SMR; Q9I4F5; -.
DR STRING; 287.DR97_751; -.
DR PaxDb; Q9I4F5; -.
DR PRIDE; Q9I4F5; -.
DR EnsemblBacteria; AAG04572; AAG04572; PA1183.
DR GeneID; 880848; -.
DR KEGG; pae:PA1183; -.
DR PATRIC; fig|208964.12.peg.1229; -.
DR PseudoCAP; PA1183; -.
DR HOGENOM; CLU_019375_7_0_6; -.
DR InParanoid; Q9I4F5; -.
DR OMA; YLYIAVI; -.
DR PhylomeDB; Q9I4F5; -.
DR BioCyc; PAER208964:G1FZ6-1208-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015138; F:fumarate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015366; F:malate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015740; P:C4-dicarboxylate transport; IDA:PseudoCAP.
DR GO; GO:0006835; P:dicarboxylic acid transport; IMP:PseudoCAP.
DR GO; GO:0070778; P:L-aspartate transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.10.3860.10; -; 1.
DR HAMAP; MF_01300; C4_dicarb_transport; 1.
DR InterPro; IPR023954; C4_dicarb_transport.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR42865; PTHR42865; 1.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..436
FT /note="C4-dicarboxylate transport protein 2"
FT /id="PRO_0000202098"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT REGION 414..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 45994 MW; DCA564DB31A5AC07 CRC64;
MTKQPFYKSL YVQVLVAIAI GIALGHWYPE TAVAMKPFGD GFVKLIKMAI APIIFCTVVT
GIAGMQSMKS VGKTGGMALL YFEVVSTVAL IIGLVVVNVV QPGAGMHVDP NTLDTSKIAA
YAAAGEKQST VDFLMNVIPG TVVGAFANGD ILQVLFFSVL FGYALHRLGS YGKPVFEFIE
RVSHVMFNII NVIMKVAPIG AFGAMAFTIG AYGVGSLVQL GQLMLCFYIT CILFVLIVLG
GIARAHGFSI LRFIRYIREE LLIVLGTSSS ESALPRMIDK MEKLGCNKSV VGLVIPTGYS
FNLDGTSIYL TMAAVFIAQA TDTPMDITHQ ITLLLVLLIA SKGAAGVTGS GFIVLAATLS
AVGHLPVAGL ALILGIDRFM SEARALTNLV GNGVATVVVS KWCKQLDEGT LQRELAGEGN
ASSPASDIPV GGREAV
