ID B7IEG8_THEAB Unreviewed; 345 AA.
AC B7IEG8;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Arsenical-resistance protein {ECO:0000313|EMBL:ACJ76395.1};
GN Name=arsB {ECO:0000313|EMBL:ACJ76395.1};
GN OrderedLocusNames=THA_1974 {ECO:0000313|EMBL:ACJ76395.1};
OS Thermosipho africanus (strain TCF52B).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Thermosipho.
OX NCBI_TaxID=484019 {ECO:0000313|EMBL:ACJ76395.1, ECO:0000313|Proteomes:UP000002453};
RN [1] {ECO:0000313|EMBL:ACJ76395.1, ECO:0000313|Proteomes:UP000002453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCF52B {ECO:0000313|EMBL:ACJ76395.1,
RC ECO:0000313|Proteomes:UP000002453};
RX PubMed=19124572; DOI=10.1128/JB.01448-08;
RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT the Firmicutes and Archaea.";
RL J. Bacteriol. 191:1974-1978(2009).
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; CP001185; ACJ76395.1; -; Genomic_DNA.
DR RefSeq; WP_012580519.1; NC_011653.1.
DR AlphaFoldDB; B7IEG8; -.
DR STRING; 484019.THA_1974; -.
DR KEGG; taf:THA_1974; -.
DR eggNOG; COG0798; Bacteria.
DR HOGENOM; CLU_022869_0_2_0; -.
DR Proteomes; UP000002453; Chromosome.
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 345 AA; 38605 MW; 48BA8426F24987D1 CRC64;
MKKKMKFFEK YLSIWVALCI IGGFLLGKIF PQVPKTLSKW EYANVSIPIA ILIWLMIYPM
MLKIDFSSIK NVGRNPKGLI ITLTVNWLIK PFTMYFIAYF FLKIVFGNII GVELSSEYVA
GAVLLGAAPC TAMVFVWSYL TNGDALYTLV QVAINDLVIL FAFAPIVSFL LKVGNITVPF
KTLIFSVVIF VLIPLIVAII TRHYVIKNKG KEYLERKFIP KFSTISIIGL LLTLILLFSF
QGETIEKNFI HILLISIPLI IQTFLIFTIG YFWAYFWKVP HSIAAPAAMI GASNFFELAV
AVAISLFGMN SGAALATVVG VLVEVPVMLT LVKIANTTRK KFKKA
//