ID M0MHW5_9EURY Unreviewed; 364 AA.
AC M0MHW5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Arsenical-resistance protein {ECO:0000313|EMBL:EMA44933.1};
GN ORFNames=C449_09759 {ECO:0000313|EMBL:EMA44933.1};
OS Halococcus saccharolyticus DSM 5350.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1227455 {ECO:0000313|EMBL:EMA44933.1, ECO:0000313|Proteomes:UP000011669};
RN [1] {ECO:0000313|EMBL:EMA44933.1, ECO:0000313|Proteomes:UP000011669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5350 {ECO:0000313|EMBL:EMA44933.1,
RC ECO:0000313|Proteomes:UP000011669};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {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}.
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:EMA44933.1}.
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DR EMBL; AOMD01000021; EMA44933.1; -; Genomic_DNA.
DR AlphaFoldDB; M0MHW5; -.
DR STRING; 1227455.C449_09759; -.
DR PATRIC; fig|1227455.4.peg.1999; -.
DR InParanoid; M0MHW5; -.
DR OrthoDB; 326456at2157; -.
DR Proteomes; UP000011669; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011669};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 364 AA; 39258 MW; 7D34F0F248AF151E CRC64;
MDFLDKYLTV WIFGAMAIGV GLGYIAPSVT EPIQNLHLVE IGLIVMMYPP LAKADYSQLR
TVFSNWRVLG LSLIQNWLIG PTLMFGLAVV FFSGLVPGLP ARPEFFLGLV FIGMARCIAM
VLVWNELAEG SPEYVTGLVA FNSLFQIVTY GVYVWFFGLF LPPLLGMDSL VAGITTFDIT
PMQVFQAIVV FLGIPFVGGF LTRYVGTHTK GEEWYDEELI PKIDPLTLVA LLFTVIVMFA
TQGENIIAAP ADVLLIAVPL TIYFVVMFFV SFGMGKGIGA DYSTTTAIGF TAASNNFELA
IAVAVAVFGV GSGVAFTTVV GPLIEVPVLL ALVNVALYFQ RNLDWGGAGT GSFDASASEP
TTDD
//
