SDAC_ECOLI
ID SDAC_ECOLI Reviewed; 429 AA.
AC P0AAD6; P36559; Q2MA38;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Serine transporter SdaC {ECO:0000303|PubMed:31680488};
DE AltName: Full=H(+)/L-serine symporter {ECO:0000305};
DE AltName: Full=L-serine transport system {ECO:0000303|PubMed:3129404};
GN Name=sdaC {ECO:0000303|PubMed:8026499};
GN Synonyms=dcrA {ECO:0000303|PubMed:8752353};
GN OrderedLocusNames=b2796, JW2767;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=8026499; DOI=10.1111/j.1432-1033.1994.tb18938.x;
RA Shao Z., Lin R.T., Newman E.B.;
RT "Sequencing and characterization of the sdaC gene and identification of the
RT sdaCB operon in Escherichia coli K12.";
RL Eur. J. Biochem. 222:901-907(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=3129404; DOI=10.1128/jb.170.5.2236-2239.1988;
RA Hama H., Shimamoto T., Tsuda M., Tsuchiya T.;
RT "Characterization of a novel L-serine transport system in Escherichia
RT coli.";
RL J. Bacteriol. 170:2236-2239(1988).
RN [5]
RP FUNCTION, FUNCTION IN PHAGE C1 INFECTION (MICROBIAL INFECTION), AND
RP DISRUPTION PHENOTYPE.
RX PubMed=8752353; DOI=10.1128/jb.178.17.5309-5315.1996;
RA Likhacheva N.A., Samsonov V.V., Samsonov V.V., Sineoky S.P.;
RT "Genetic control of the resistance to phage C1 of Escherichia coli K-12.";
RL J. Bacteriol. 178:5309-5315(1996).
RN [6]
RP FUNCTION IN PHAGE INFECTION (MICROBIAL INFECTION), AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12558182; DOI=10.1016/s0923-2508(02)01375-x;
RA Samsonov V.V., Samsonov V.V., Sineoky S.P.;
RT "DcrA and dcrB Escherichia coli genes can control DNA injection by phages
RT specific for BtuB and FhuA receptors.";
RL Res. Microbiol. 153:639-646(2002).
RN [7]
RP FUNCTION AS A COLV RECEPTOR (MICROBIAL INFECTION), AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15743941; DOI=10.1128/jb.187.6.1945-1950.2005;
RA Gerard F., Pradel N., Wu L.F.;
RT "Bactericidal activity of colicin V is mediated by an inner membrane
RT protein, SdaC, of Escherichia coli.";
RL J. Bacteriol. 187:1945-1950(2005).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [9]
RP OPERON STRUCTURE, AND INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=19429622; DOI=10.1128/jb.00108-09;
RA Shimada T., Yamamoto K., Ishihama A.;
RT "Involvement of the leucine response transcription factor LeuO in
RT regulation of the genes for sulfa drug efflux.";
RL J. Bacteriol. 191:4562-4571(2009).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
RX PubMed=31680488; DOI=10.1002/mbo3.960;
RA Kriner M.A., Subramaniam A.R.;
RT "The serine transporter SdaC prevents cell lysis upon glucose depletion in
RT Escherichia coli.";
RL MicrobiologyOpen 9:e960-e960(2020).
CC -!- FUNCTION: Mediates the import of L-serine into the cell
CC (PubMed:8026499, PubMed:3129404). Is energized by proton cotransport
CC (PubMed:3129404). Promotes amino acid homeostasis during adaptation to
CC glucose limitation (PubMed:31680488). May also be involved in
CC ampicillin sensitivity (Probable). {ECO:0000269|PubMed:3129404,
CC ECO:0000269|PubMed:31680488, ECO:0000269|PubMed:8026499,
CC ECO:0000305|PubMed:8752353}.
CC -!- FUNCTION: (Microbial infection) Involved in phage C1 and phage C6
CC infection (PubMed:8752353, PubMed:12558182). Participates in phage DNA
CC transport pathways in cooperation with different outer membrane
CC receptors, including FhuA and BtuB (PubMed:12558182). Is probably
CC required in the second stage of phage adsorption, the DNA injection
CC process. Participates in the formation or opening of diffusion channels
CC through the outer membrane after phage adsorption (PubMed:12558182).
CC {ECO:0000269|PubMed:12558182, ECO:0000269|PubMed:8752353}.
CC -!- FUNCTION: (Microbial infection) May function as an inner membrane
CC receptor of colicin V (ColV), a peptide antibiotic secreted by some
CC members of the Enterobacteriaceae to kill closely related bacterial
CC cells. {ECO:0000269|PubMed:15743941}.
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:0000269|PubMed:3129404};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28889;
CC Evidence={ECO:0000269|PubMed:3129404};
CC -!- ACTIVITY REGULATION: Serine transport is strongly inhibited by KCN, an
CC inhibitor of the respiratory chain, or by CCCP.
CC {ECO:0000269|PubMed:3129404}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for L-serine {ECO:0000269|PubMed:3129404};
CC Vmax=23 nmol/min/mg enzyme {ECO:0000269|PubMed:3129404};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: By leucine and by growth in rich medium (PubMed:3129404,
CC PubMed:19429622). Repressed by LeuO. Part of the sdaCB operon
CC (PubMed:19429622). {ECO:0000269|PubMed:19429622,
CC ECO:0000269|PubMed:3129404}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene leads to phage C1
CC adsorption defect. Mutation does not impair vitamin B12 utilization.
CC Inactivation also leads to increased ampicillin resistance
CC (PubMed:8752353). Mutant is resistant to phage C6 (PubMed:12558182).
CC Mutation also confers resistance to ColV (PubMed:15743941). Deletion
CC mutant lyses upon glucose depletion in the absence of exogenous serine
CC (PubMed:31680488). {ECO:0000269|PubMed:12558182,
CC ECO:0000269|PubMed:15743941, ECO:0000269|PubMed:31680488,
CC ECO:0000269|PubMed:8752353}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC SdaC/TdcC subfamily. {ECO:0000305}.
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DR EMBL; U01233; AAA50169.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40446.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75838.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76868.1; -; Genomic_DNA.
DR PIR; S45633; S45633.
DR RefSeq; NP_417276.1; NC_000913.3.
DR RefSeq; WP_000450476.1; NZ_STEB01000030.1.
DR AlphaFoldDB; P0AAD6; -.
DR BioGRID; 4261307; 23.
DR STRING; 511145.b2796; -.
DR TCDB; 2.A.42.2.1; the hydroxy/aromatic amino acid permease (haaap) family.
DR jPOST; P0AAD6; -.
DR PaxDb; P0AAD6; -.
DR PRIDE; P0AAD6; -.
DR EnsemblBacteria; AAC75838; AAC75838; b2796.
DR EnsemblBacteria; BAE76868; BAE76868; BAE76868.
DR GeneID; 66673337; -.
DR GeneID; 947264; -.
DR KEGG; ecj:JW2767; -.
DR KEGG; eco:b2796; -.
DR PATRIC; fig|1411691.4.peg.3937; -.
DR EchoBASE; EB2063; -.
DR eggNOG; COG0814; Bacteria.
DR HOGENOM; CLU_052043_1_1_6; -.
DR OMA; PLTYLGH; -.
DR PhylomeDB; P0AAD6; -.
DR BioCyc; EcoCyc:SDAC-MON; -.
DR BioCyc; MetaCyc:SDAC-MON; -.
DR PRO; PR:P0AAD6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; ISM:EcoCyc.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015825; P:L-serine transport; IMP:EcoCyc.
DR InterPro; IPR004694; Hydroxy_aa_transpt.
DR TIGRFAMs; TIGR00814; stp; 1.
PE 1: Evidence at protein level;
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_0000093808"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..46
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..140
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..201
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..297
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..429
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 429 AA; 46906 MW; F97AB93F84A38FE6 CRC64;
METTQTSTIA SKDSRSAWRK TDTMWMLGLY GTAIGAGVLF LPINAGVGGM IPLIIMAILA
FPMTFFAHRG LTRFVLSGKN PGEDITEVVE EHFGIGAGKL ITLLYFFAIY PILLVYSVAI
TNTVESFMSH QLGMTPPPRA ILSLILIVGM MTIVRFGEQM IVKAMSILVF PFVGVLMLLA
LYLIPQWNGA ALETLSLDTA SATGNGLWMT LWLAIPVMVF SFNHSPIISS FAVAKREEYG
DMAEQKCSKI LAFAHIMMVL TVMFFVFSCV LSLTPADLAA AKEQNISILS YLANHFNAPV
IAWMAPIIAI IAITKSFLGH YLGAREGFNG MVIKSLRGKG KSIEINKLNR ITALFMLVTT
WIVATLNPSI LGMIETLGGP IIAMILFLMP MYAIQKVPAM RKYSGHISNV FVVVMGLIAI
SAIFYSLFS
