ID Q3YS16_EHRCJ Unreviewed; 426 AA.
AC Q3YS16;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Sodium:dicarboxylate symporter {ECO:0000313|EMBL:AAZ68489.1};
GN OrderedLocusNames=Ecaj_0449 {ECO:0000313|EMBL:AAZ68489.1};
OS Ehrlichia canis (strain Jake).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484 {ECO:0000313|EMBL:AAZ68489.1, ECO:0000313|Proteomes:UP000000435};
RN [1] {ECO:0000313|Proteomes:UP000000435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake {ECO:0000313|Proteomes:UP000000435};
RX PubMed=16707693; DOI=10.1128/JB.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000256|ARBA:ARBA00006148}.
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DR EMBL; CP000107; AAZ68489.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YS16; -.
DR STRING; 269484.Ecaj_0449; -.
DR KEGG; ecn:Ecaj_0449; -.
DR eggNOG; COG1301; Bacteria.
DR HOGENOM; CLU_019375_7_1_5; -.
DR InParanoid; Q3YS16; -.
DR Proteomes; UP000000435; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015293; F:symporter activity; IEA:InterPro.
DR Gene3D; 1.10.3860.10; Sodium:dicarboxylate symporter; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR42865:SF5; L-CYSTINE TRANSPORTER TCYP; 1.
DR PANTHER; PTHR42865; PROTON/GLUTAMATE-ASPARTATE SYMPORTER; 1.
DR Pfam; PF00375; SDF; 1.
DR PRINTS; PR00173; EDTRNSPORT.
DR SUPFAM; SSF118215; Proton glutamate symport protein; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 426 AA; 47904 MW; AB07E6A0146E2D73 CRC64;
MINRNLLNIT CNFVLLMIHK FSLKIFIPII LAIISYYVNQ KWIFEFAKAF GDIFINLLKL
ISLPVVFFSI TSTISGLANL IEIKNLIKKT IFYTISTTIV AAIIALTIYL LIDPSKKALV
FNILNTNEHI NTPDYLSYLI SILPHNFIKV FLDNNVIGCV ILAFLIGGSL LVLPDKNKRE
LLHKILDALF DTFLEIAKLI LKLMPIALWS FITVLLYNTK EGYNLSSILK YLLCIMVANF
IQAFVVLPLL LKLKKISVIK TFRGALPALT IAFFSKSSTA TLPTTLRCAQ DNLKISKKIS
SFILPVCTTI NMNACAAFIL ITVFFVSEMN EYTFSIGEMF LWIFLATGAA IGNAGVPMGC
YFMAMSYLIS MKVPLSIMGI ILPIYTIIDM FETAINVWSD VCIAQVINKE YSILTQENKK
ISHNTK
//
