ID Q83L44_SHIFL Unreviewed; 355 AA.
AC Q83L44;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 113.
DE SubName: Full=Transporter {ECO:0000313|EMBL:AAN43092.1};
GN OrderedLocusNames=SF1501 {ECO:0000313|EMBL:AAN43092.1};
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623 {ECO:0000313|EMBL:AAN43092.1, ECO:0000313|Proteomes:UP000001006};
RN [1] {ECO:0000313|EMBL:AAN43092.1, ECO:0000313|Proteomes:UP000001006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a {ECO:0000313|Proteomes:UP000001006};
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).
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; AE005674; AAN43092.1; -; Genomic_DNA.
DR AlphaFoldDB; Q83L44; -.
DR PaxDb; 198214-SF1501; -.
DR KEGG; sft:NCTC1_01619; -.
DR PATRIC; fig|623.156.peg.429; -.
DR HOGENOM; CLU_019375_0_0_6; -.
DR Proteomes; UP000001006; 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 Reference proteome {ECO:0000313|Proteomes:UP000001006};
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 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 355 AA; 37876 MW; 9C1773A1B91174AA CRC64;
MNFPLIANIV VFVVLLFALA QTRHKQWSLA KKVLVGLVMG VVFGLALHTI YGSDSQVLKD
SVQWFNIVGN GYVQLLQMIV MPLVFASILS AVARLHNASQ LGKISFLTIG TLLFTTLIAA
LVGVLVTNLF GLTAEGLVQG GAETARLNAI ESNYVGKVSD QSVPQLVLSF IPKNPFADLT
GANPTSIISV VIFAAFLGVA ALKLLKDDAP KGERVLTAID TLQSWVMKLV RLVMQLTPYG
VLALMTKVVA GSNLQDIIKL GSFVVASYLG LLIMFAVHGI LLGINGVSPL KYFRKVWPVL
TFAFTSRSSA ASIPLNVEAQ TRRLGVPESI ASFAASFGAT IGQNGCAGLY PAMLR
//
