ID A0A196NFY1_9SPHN Unreviewed; 359 AA.
AC A0A196NFY1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Arsenical-resistance protein {ECO:0000313|EMBL:OAN66764.1};
GN ORFNames=A7X12_11365 {ECO:0000313|EMBL:OAN66764.1};
OS Sphingomonas sp. TDK1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=453247 {ECO:0000313|EMBL:OAN66764.1, ECO:0000313|Proteomes:UP000078445};
RN [1] {ECO:0000313|EMBL:OAN66764.1, ECO:0000313|Proteomes:UP000078445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TDK1 {ECO:0000313|EMBL:OAN66764.1,
RC ECO:0000313|Proteomes:UP000078445};
RA Takahashi S.;
RT "Draft Genome Sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp.
RT strain TDK1, Haloalkyl Organophosphorus Flame Retardant-Degrading
RT Bacteria.";
RL Submitted (MAY-2016) 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}.
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:OAN66764.1}.
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DR EMBL; LXVY01000003; OAN66764.1; -; Genomic_DNA.
DR RefSeq; WP_064310280.1; NZ_LXVY01000003.1.
DR AlphaFoldDB; A0A196NFY1; -.
DR STRING; 453247.A7X12_11365; -.
DR OrthoDB; 5290400at2; -.
DR Proteomes; UP000078445; 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.
DR PRINTS; PR00173; EDTRNSPORT.
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 23..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 359 AA; 37607 MW; BBC0EAB34AACEAFD CRC64;
MSTVSPTLDA APARPGIGTF ERYLTLLVLL CIAAGIGLGQ LLPGVFASIV AAEVARVNLI
VAMLIWLMII PMLLKIDFGA LGSVRQHWKG VGVTLFINWA VKPFSMAALG TLFIGWLFAP
LLPAGEGPSY IAGLILLAAA PCTAMVFVWS NLCEGEPTYT LSQVALNDVL MVFLFAPLVG
LLLGVASVTV PWDTLLISVL LYIVVPVIAA QLVRRAVLAR GGQAALDRLL ARLGPVSLVA
LLATLVLLFG FQGEAIVAQP LVIALLAVPI LIQVYLNAGL AYWLSRRFGV AWCVAAPAAL
IGASNFFELA VAAAISLFGL KSGAALATVV GVLVEVPVML SVVSIVKASR GWYERGTAA
//