SDCS_STAAM
ID SDCS_STAAM Reviewed; 520 AA.
AC Q99SX1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Sodium-dependent dicarboxylate transporter SdcS;
DE AltName: Full=Na(+)/dicarboxylate symporter;
GN Name=sdcS; OrderedLocusNames=SAV1916;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16030212; DOI=10.1128/jb.187.15.5189-5194.2005;
RA Hall J.A., Pajor A.M.;
RT "Functional characterization of a Na(+)-coupled dicarboxylate carrier
RT protein from Staphylococcus aureus.";
RL J. Bacteriol. 187:5189-5194(2005).
RN [3]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17114260; DOI=10.1128/jb.01452-06;
RA Hall J.A., Pajor A.M.;
RT "Functional reconstitution of SdcS, a Na+-coupled dicarboxylate carrier
RT protein from Staphylococcus aureus.";
RL J. Bacteriol. 189:880-885(2007).
CC -!- FUNCTION: Mediates the transport of the dicarboxylates fumarate,
CC malate, and succinate across the cytoplasmic membrane via a Na(+)-
CC electrochemical gradient. Transports 2 Na(+) for each dicarboxylate.
CC {ECO:0000269|PubMed:16030212, ECO:0000269|PubMed:17114260}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for fumarate (in the presence of 5 mM Na(+))
CC {ECO:0000269|PubMed:16030212, ECO:0000269|PubMed:17114260};
CC KM=8.1 uM for malate (in the presence of 5 mM Na(+))
CC {ECO:0000269|PubMed:16030212, ECO:0000269|PubMed:17114260};
CC KM=4.5 uM for succinate {ECO:0000269|PubMed:16030212,
CC ECO:0000269|PubMed:17114260};
CC KM=12 uM for succinate (in the presence of saturating concentrations
CC of Na(+)) {ECO:0000269|PubMed:16030212, ECO:0000269|PubMed:17114260};
CC KM=2.7 mM for Na(+) {ECO:0000269|PubMed:16030212,
CC ECO:0000269|PubMed:17114260};
CC Vmax=16 nmol/min/mg enzyme toward fumarate (in the presence of 5 mM
CC Na(+)) {ECO:0000269|PubMed:16030212, ECO:0000269|PubMed:17114260};
CC Vmax=12 nmol/min/mg enzyme toward malate (in the presence of 5 mM
CC Na(+)) {ECO:0000269|PubMed:16030212, ECO:0000269|PubMed:17114260};
CC Vmax=17 nmol/min/mg enzyme toward succinate (in the presence of 5 mM
CC Na(+)) {ECO:0000269|PubMed:16030212, ECO:0000269|PubMed:17114260};
CC Vmax=1.8 umol/min/mg enzyme toward succinate (in the presence of
CC saturating concentrations of Na(+)) {ECO:0000269|PubMed:16030212,
CC ECO:0000269|PubMed:17114260};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: The binding of Na(+) at the extracellular surface
CC probably precedes the binding of dicarboxylate, since there is a
CC competitive activation of succinate transport by Na(+) and an
CC uncompetitive nature of succinate on Na(+) affinity.
CC -!- SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) family.
CC NADC subfamily. {ECO:0000305}.
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; BA000017; BAB58078.1; -; Genomic_DNA.
DR RefSeq; WP_000323161.1; NC_002758.2.
DR AlphaFoldDB; Q99SX1; -.
DR SMR; Q99SX1; -.
DR PaxDb; Q99SX1; -.
DR EnsemblBacteria; BAB58078; BAB58078; SAV1916.
DR KEGG; sav:SAV1916; -.
DR HOGENOM; CLU_005170_0_0_9; -.
DR OMA; LHGMNTY; -.
DR PhylomeDB; Q99SX1; -.
DR BioCyc; SAUR158878:SAV_RS10500-MON; -.
DR Proteomes; UP000002481; 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-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR001898; SLC13A/DASS.
DR Pfam; PF00939; Na_sulph_symp; 1.
DR TIGRFAMs; TIGR00785; dass; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion transport; Membrane; Sodium; Sodium transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..520
FT /note="Sodium-dependent dicarboxylate transporter SdcS"
FT /id="PRO_0000260095"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 520 AA; 57172 MW; 77F87F2B1B1C404A CRC64;
MAYFNQHQSM ISKRYLTFFS KSKKKKPFSA GQLIGLILGP LLFLLTLLFF HPQDLPWKGV
YVLAITLWIA TWWITEAIPI AATSLLPIVL LPLGHILTPE QVSSEYGNDI IFLFLGGFIL
AIAMERWNLH TRVALTIINL IGASTSKILL GFMVATGFLS MFVSNTAAVM IMIPIGLAII
KEAHDLQEAN TNQTSIQKFE KSLVLAIGYA GTIGGLGTLI GTPPLIILKG QYMQHFGHEI
SFAKWMIVGI PTVIVLLGIT WLYLRYVAFR HDLKYLPGGQ TLIKQKLDEL GKMKYEEKVV
QTIFVLASLL WITREFLLKK WEVTSSVADG TIAIFISILL FIIPAKNTEK HRRIIDWEVA
KELPWGVLIL FGGGLALAKG ISESGLAKWL GEQLKSLNGV SPILIVIVIT IFVLFLTEVT
SNTATATMIL PILATLSVAV GVHPLLLMAP AAMAANCAYM LPVGTPPNAI IFGSGKISIK
QMASVGFWVN LISAIIIILV VYYVMPIVLG IDINQPLPLK
