DCTM_PSEAE
ID DCTM_PSEAE Reviewed; 427 AA.
AC Q9HU16;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=C4-dicarboxylate TRAP transporter large permease protein DctM {ECO:0000305};
GN Name=dctM {ECO:0000303|PubMed:21725012}; OrderedLocusNames=PA5169;
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, SUBUNIT, 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: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system DctPQM involved in C4-dicarboxylates uptake.
CC {ECO:0000269|PubMed:21725012}.
CC -!- SUBUNIT: The complex comprises the extracytoplasmic solute receptor
CC protein DctP, and the two transmembrane proteins DctQ and DctM.
CC {ECO:0000305|PubMed:21725012}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:O07838}; Multi-pass membrane protein
CC {ECO:0000255}.
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 regulated by DctA. {ECO:0000269|PubMed:21725012}.
CC -!- DISRUPTION PHENOTYPE: The dctA-dctPQM double mutant shows no growth on
CC malate and fumarate and residual growth on succinate.
CC {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 TRAP transporter large permease family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG08554.1; -; Genomic_DNA.
DR PIR; B83001; B83001.
DR RefSeq; NP_253856.1; NC_002516.2.
DR RefSeq; WP_003105529.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HU16; -.
DR SMR; Q9HU16; -.
DR STRING; 287.DR97_2537; -.
DR PaxDb; Q9HU16; -.
DR PRIDE; Q9HU16; -.
DR EnsemblBacteria; AAG08554; AAG08554; PA5169.
DR GeneID; 877773; -.
DR KEGG; pae:PA5169; -.
DR PATRIC; fig|208964.12.peg.5417; -.
DR PseudoCAP; PA5169; -.
DR HOGENOM; CLU_019824_4_1_6; -.
DR InParanoid; Q9HU16; -.
DR OMA; IVVNMEV; -.
DR PhylomeDB; Q9HU16; -.
DR BioCyc; PAER208964:G1FZ6-5286-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015740; P:C4-dicarboxylate transport; IMP:PseudoCAP.
DR InterPro; IPR010656; DctM.
DR InterPro; IPR004681; TRAP_DctM.
DR PANTHER; PTHR33362; PTHR33362; 1.
DR Pfam; PF06808; DctM; 1.
DR PIRSF; PIRSF006066; HI0050; 1.
DR TIGRFAMs; TIGR00786; dctM; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..427
FT /note="C4-dicarboxylate TRAP transporter large permease
FT protein DctM"
FT /id="PRO_0000435378"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 427 AA; 45202 MW; 6065845F1BC91829 CRC64;
MTILFLFLLL FLLMFIGVPI AVSLGLSGAL TILLFSPDSV RSLAIKLFET SEHYTLLAIP
FFLLSGAFMT TGGVARRLID FANACVGHIR GGLAIAAVLA CMLFAALSGS SPATVAAVGS
IAIAGMVRSG YPQAFGAGIV CNAGTLGILI PPSIVMVVYA AATETSVGKL FIAGVVPGLL
LGLILMVVIY IVARVKKLPA MPRVSLREWL ASARKALWGL LLMVIILGGI YSGAFTPTEA
AAVAAVYSAF VALFVYRDMR LSECPKVLLE SGKLTIMLMF IIANAMLFAH VLTTEQIPQS
IASWVTELGL SPWMFLLVVN IVLLIAGNFM EPSAIILILA PIFFPIAMEL GIDPIHLGII
MVVNMEIGLI TPPVGLNLFV TSAVTGMPLG ATIRAALPWL MILLVFLIIV TYIPAVSLAL
PNWLGMS
