ID A0A1E4HEJ0_9GAMM Unreviewed; 359 AA.
AC A0A1E4HEJ0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Arsenical-resistance protein {ECO:0000313|EMBL:ODT95308.1};
GN ORFNames=ABS82_08530 {ECO:0000313|EMBL:ODT95308.1};
OS Rhodanobacter sp. SCN 67-45.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1660133 {ECO:0000313|EMBL:ODT95308.1, ECO:0000313|Proteomes:UP000094158};
RN [1] {ECO:0000313|EMBL:ODT95308.1, ECO:0000313|Proteomes:UP000094158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODT95308.1}.
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DR EMBL; MEFB01000047; ODT95308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4HEJ0; -.
DR Proteomes; UP000094158; 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 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 25..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 359 AA; 38712 MW; CA1BCF1869226141 CRC64;
MTQLNVDTVA ADQPVPARIG FFERYLTVWV LLCIVVGTLL GHLLPGSFEA LGSMSVAQVN
LPVAVLIWLM IIPMLLKIDF GAMAGVRRQW KGIGVTLFIN WAVKPFSMAL LGWIFIRHVF
AGYLPADQLD SYIAGLILLA AAPCTAMVFV WSNLCNGEPN FTLSQVALND AIMVVAFAPI
VALLLGISSI TVPWNTLFLS VLLYIVVPVA ISVALRRWML SHGGPDKLQA MLHRLGPVSL
VALLATLVLL FGFQGQQILE QPAIIAMLAM PILIQVYFNS GLAYLLNRRF GVPHCVAGPS
ALIGASNFFE LAVATAVGLF GVHSGAALAT VVGVLIEVPV MLSVVRIVNR SRGWYEARA
//