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Database: UniProt
Entry: A0A239AV31_9FIRM
LinkDB: A0A239AV31_9FIRM
Original site: A0A239AV31_9FIRM 
ID   A0A239AV31_9FIRM        Unreviewed;       356 AA.
AC   A0A239AV31;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Arsenite transporter, ACR3 family {ECO:0000313|EMBL:SNR98894.1};
GN   ORFNames=SAMN05446037_1002253 {ECO:0000313|EMBL:SNR98894.1};
OS   Anaerovirgula multivorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Anaerovirgula.
OX   NCBI_TaxID=312168 {ECO:0000313|EMBL:SNR98894.1, ECO:0000313|Proteomes:UP000198304};
RN   [1] {ECO:0000313|EMBL:SNR98894.1, ECO:0000313|Proteomes:UP000198304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCA {ECO:0000313|EMBL:SNR98894.1,
RC   ECO:0000313|Proteomes:UP000198304};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC       ECO:0000256|PIRNR:PIRNR005508}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|PIRNR:PIRNR005508}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59)
CC       family. {ECO:0000256|ARBA:ARBA00010110, ECO:0000256|PIRNR:PIRNR005508}.
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DR   EMBL; FZOJ01000002; SNR98894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239AV31; -.
DR   OrthoDB; 9771457at2; -.
DR   Proteomes; UP000198304; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015103; F:inorganic anion transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1530.20; -; 1.
DR   InterPro; IPR004706; Arsenical-R_Acr3.
DR   InterPro; IPR002657; BilAc:Na_symport/Acr3.
DR   InterPro; IPR038770; Na+/solute_symporter_sf.
DR   NCBIfam; TIGR00832; acr3; 1.
DR   PANTHER; PTHR43057:SF1; ARSENICAL-RESISTANCE PROTEIN 3; 1.
DR   PANTHER; PTHR43057; ARSENITE EFFLUX TRANSPORTER; 1.
DR   Pfam; PF01758; SBF; 1.
DR   PIRSF; PIRSF005508; Acr3; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR005508};
KW   Membrane {ECO:0000256|PIRNR:PIRNR005508, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198304};
KW   Transmembrane {ECO:0000256|PIRNR:PIRNR005508, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|PIRNR:PIRNR005508,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR005508}.
FT   TRANSMEM        12..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        229..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        293..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   356 AA;  39095 MW;  719D2665E34B746E CRC64;
     MSQNQEQKGA GLGFFETYLT VWVALCIIIG VAIGQFLPIV PDVLSQFEYA QVSIPVAILI
     WLMIYPMMLK IDFTSIVEAT KKPKGLIVTC VINWLIKPFT MYLIAAFFLK VVFQNFIPEA
     LANDYLAGAV LLGAAPCTAM VFVWSHLTKG DPAYTLVQVA VNDLILLVAF TPIVALLLGI
     TDVFVPYDTL FLSVVLFIVI PLAGGYLSRK YIVQKEGIEY FENVFLKKFD NVTIVGLLLT
     LIIIFTFQGD VILSNPLHIL LIAIPLTIQT FFIFALAYGW ARAWKLPHNV ASPAAMIGAS
     NFFELAVAVA ISLFGLTSGA TLATVVGVLV EVPVMLALVR IANNTRHWFP QVSKGN
//
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