SDAC_SHIFL
ID SDAC_SHIFL Reviewed; 429 AA.
AC Q83QD0;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Serine transporter SdaC {ECO:0000250|UniProtKB:P0AAD6};
DE AltName: Full=H(+)/L-serine symporter {ECO:0000250|UniProtKB:P0AAD6};
GN Name=sdaC; OrderedLocusNames=SF2810, S3005;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Mediates the import of L-serine into the cell. Is energized
CC by proton cotransport. {ECO:0000250|UniProtKB:P0AAD6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-serine(in) = H(+)(out) + L-serine(out);
CC Xref=Rhea:RHEA:28887, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384;
CC Evidence={ECO:0000250|UniProtKB:P0AAD6};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28889;
CC Evidence={ECO:0000250|UniProtKB:P0AAD6};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AAD6}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC SdaC/TdcC subfamily. {ECO:0000305}.
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DR EMBL; AE005674; AAN44298.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18123.1; -; Genomic_DNA.
DR RefSeq; NP_708591.1; NC_004337.2.
DR AlphaFoldDB; Q83QD0; -.
DR STRING; 198214.SF2810; -.
DR EnsemblBacteria; AAN44298; AAN44298; SF2810.
DR EnsemblBacteria; AAP18123; AAP18123; S3005.
DR GeneID; 1025784; -.
DR KEGG; sfl:SF2810; -.
DR KEGG; sfx:S3005; -.
DR PATRIC; fig|198214.7.peg.3344; -.
DR HOGENOM; CLU_052043_1_1_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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:0015171; F:amino acid transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR InterPro; IPR004694; Hydroxy_aa_transpt.
DR TIGRFAMs; TIGR00814; stp; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..429
FT /note="Serine transporter SdaC"
FT /id="PRO_0000093811"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..46
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..140
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..201
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..297
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..429
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 235
FT /note="N -> K (in Ref. 2; AAP18123)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..264
FT /note="EMI -> VMF (in Ref. 2; AAP18123)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="I -> S (in Ref. 2; AAP18123)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="H -> Q (in Ref. 2; AAP18123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 46923 MW; 7EE7A4DC9EDD2C3C CRC64;
METTQTSTIA SKDSRSAWRK TDTMWMLGLY GTAIGAGVLF LPINAGVGGM IPLIIMAILA
FPMTFFAHRG LTRFVLSGKN PGEDITEVVE EHFGIGAGKL ITLLYFFAIY PILLVYSVAI
TNTVESFMSH QLGMTPPPRA ILSLILIVGM MTIVRFGEQM IVKAMSILVF PFVGVLMLLA
LYLIPQWNGA ALETLSLDTA SATGNGLWMT LWLAIPVMVF SFNHSPIISS FAVANREEYG
DMAEQKCSKI LAFAHIMMVL TEMIFVFICV LSLTPADLAA AKEHNISILS YLANHFNAPV
IAWMAPIIAI IAITKSFLGH YLGAREGFNG MVIKSLRGKG KSIEINKLNR ITALFMLVTT
WIVATLNPSI LGMIETLGGP IIAMILFLMP MYAIQKVPAM RKYSGHISNV FVVVMGLIAI
SAIFYSLFS
