ID   DAGA_PSEHA              Reviewed;         542 AA.
AC   P30144;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Na(+)-linked D-alanine glycine permease {ECO:0000303|PubMed:1447975};
DE   AltName: Full=Sodium/alanine symporter {ECO:0000305};
GN   Name=dagA {ECO:0000303|PubMed:1447975};
OS   Pseudoalteromonas haloplanktis (Alteromonas haloplanktis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=228;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 19855 / CIP 104258 / JCM 20771 / LMG 2874 / NCIMB 19 / B-16;
RX   PubMed=1447975; DOI=10.1111/j.1365-2958.1992.tb01444.x;
RA   Macleod P.R., Macleod R.A.;
RT   "Identification and sequence of a Na(+)-linked gene from the marine
RT   bacterium Alteromonas haloplanktis which functionally complements the dagA
RT   gene of Escherichia coli.";
RL   Mol. Microbiol. 6:2673-2681(1992).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 19855 / CIP 104258 / JCM 20771 / LMG 2874 / NCIMB 19 / B-16;
RX   PubMed=3512524; DOI=10.1128/jb.165.3.825-830.1986;
RA   MacLeod P.R., MacLeod R.A.;
RT   "Cloning in Escherichia coli K-12 of a Na+-dependent transport system from
RT   a marine bacterium.";
RL   J. Bacteriol. 165:825-830(1986).
CC   -!- FUNCTION: Catalyzes the sodium-dependent uptake of extracellular D-
CC       alanine and glycine. {ECO:0000269|PubMed:1447975,
CC       ECO:0000269|PubMed:3512524}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-alanine(in) + Na(+)(in) = D-alanine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:71447, ChEBI:CHEBI:29101, ChEBI:CHEBI:57416;
CC         Evidence={ECO:0000269|PubMed:1447975, ECO:0000269|PubMed:3512524};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71449;
CC         Evidence={ECO:0000305|PubMed:1447975};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine(in) + Na(+)(in) = glycine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:68228, ChEBI:CHEBI:29101, ChEBI:CHEBI:57305;
CC         Evidence={ECO:0000269|PubMed:1447975};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68230;
CC         Evidence={ECO:0000305|PubMed:1447975};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the alanine or glycine:cation symporter (AGCS)
CC       (TC 2.A.25) family. {ECO:0000305}.
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DR   EMBL; M59081; AAA21984.1; -; Genomic_DNA.
DR   PIR; S25276; S25276.
DR   AlphaFoldDB; P30144; -.
DR   SMR; P30144; -.
DR   TCDB; 2.A.25.1.1; the alanine or glycine:cation symporter (agcs) family.
DR   eggNOG; COG1115; Bacteria.
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:0015655; F:alanine:sodium symporter activity; IEA:InterPro.
DR   InterPro; IPR001463; Na/Ala_symport.
DR   PANTHER; PTHR30330; PTHR30330; 2.
DR   Pfam; PF01235; Na_Ala_symp; 1.
DR   PRINTS; PR00175; NAALASMPORT.
DR   TIGRFAMs; TIGR00835; agcS; 1.
DR   PROSITE; PS00873; NA_ALANINE_SYMP; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Ion transport; Membrane; Sodium;
KW   Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..542
FT                   /note="Na(+)-linked D-alanine glycine permease"
FT                   /id="PRO_0000161564"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        477..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        498..518
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   542 AA;  59023 MW;  045D274C013F926F CRC64;
     MLGGAVWFPY VLLGVGLFFT IYLKFPQIRY FKHACQVVSG KFDKKDTEGD TTHFQALATA
     LSGTVGTGNI GGVALAISIG GPAALFWMWM TAFFGMTTKF VEVTLSHKYR EKTEDGTMSG
     GPMYYMDKRL NMKWLAILFA VATVISSFGT GSLPQINNIA QGMEATFGFA PMATGAVLSI
     LLALVILGGI KRIAAITSRV VPLMAAIYII GALAVIFYNA ENIGPSFSAV FMDAFSGSAA
     AGGFLGASFA YAFNRGVNRG LFSNEAGQGS APIAHASAKA DEPVSEGIVS ILEPFIDTII
     ICTLTGLVIL SSGVWNEKFQ THFERSAMSI IKGDYTEENQ TQREDLYKYL NGQKSNIETF
     TGNIEVVNGE ALSTGFTVLH SRSIAEDVRF GITEKHKYTG VVEVIDGMPT DDSISLVGKS
     LVHSAELTTK AFKRGYFGDS GQYIVSIGLL LFAFSTAIAW SYYGDRAMIY LLGHRSVMPY
     RVFYVAAFFW ASFADTTLVW KLAAVAIVVM TLPNLIGIML LRKEMKESVD DYWVKFKKDN
     EK