DCTA_ALBFT
ID DCTA_ALBFT Reviewed; 448 AA.
AC Q21YI0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=C4-dicarboxylate transport protein {ECO:0000255|HAMAP-Rule:MF_01300};
GN Name=dctA {ECO:0000255|HAMAP-Rule:MF_01300}; OrderedLocusNames=Rfer_1440;
OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS (Rhodoferax ferrireducens).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=338969;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for the transport of dicarboxylates such as
CC succinate, fumarate, and malate from the periplasm across the membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01300}.
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 -!- 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; CP000267; ABD69173.1; -; Genomic_DNA.
DR RefSeq; WP_011463741.1; NC_007908.1.
DR AlphaFoldDB; Q21YI0; -.
DR SMR; Q21YI0; -.
DR STRING; 338969.Rfer_1440; -.
DR EnsemblBacteria; ABD69173; ABD69173; Rfer_1440.
DR KEGG; rfr:Rfer_1440; -.
DR eggNOG; COG1301; Bacteria.
DR HOGENOM; CLU_019375_7_0_4; -.
DR OMA; VAMKKPQ; -.
DR OrthoDB; 781228at2; -.
DR Proteomes; UP000008332; 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:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006835; P:dicarboxylic acid transport; IEA:UniProtKB-UniRule.
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; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..448
FT /note="C4-dicarboxylate transport protein"
FT /id="PRO_0000321997"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
SQ SEQUENCE 448 AA; 47750 MW; 074AB58A0F17A06E CRC64;
MSKTSARKPL YKSLYAQVIF AVTIGVLLGH FYPQLGTQMK PLGDGFIKLI KMIIAPIIFC
TVVVGIAGME DMKKVGKTGG LALLYFEVMS TLALVVGLLV VNVLQPGTGM HVDPMSLDTK
GIAAYTAPGK MQGSVDFLLN VIPSSVVDAF AKGEILQVLL FSVLFGFALH KFGGRGTMVF
DFIEKFSHVL FDIVGIIMKV APIGAFGAMA FTIGKYGLGS LFSLGKLMGA FYLTCLIFVF
GVLGIVSRLN GFSVFKFVRY IKEELLIVLG TSSSESVLPR MMEKMENLGA RKSVVGLVIP
TGYSFNLDGT SIYLTMAAVF IAQATDTPMT LMQQVTLLAV LLLTSKGAAG VTGSGFIVLA
ATLSAVGGVP VAGLALILGI DRFMSEARAL TNLVGNGVAT LVVAKWTGDL DMTRLHQGLD
NPTTRESQEP EAILDLQVTH MDVMKAKN