ARSB_STAXY
ID ARSB_STAXY Reviewed; 429 AA.
AC Q01255;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Arsenical pump membrane protein;
DE AltName: Full=Arsenic efflux pump protein;
GN Name=arsB;
OS Staphylococcus xylosus.
OG Plasmid pSX267.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1288;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 20267 / Isolate C2A;
RX PubMed=1534327; DOI=10.1128/jb.174.11.3676-3683.1992;
RA Rosenstein R., Peschel A., Wieland B., Goetz F.;
RT "Expression and regulation of the antimonite, arsenite, and arsenate
RT resistance operon of Staphylococcus xylosus plasmid pSX267.";
RL J. Bacteriol. 174:3676-3683(1992).
CC -!- FUNCTION: Involved in arsenical resistance. Thought to form the channel
CC of an arsenite pump.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ArsB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M80565; AAA27588.1; -; Genomic_DNA.
DR PIR; B41902; B41902.
DR AlphaFoldDB; Q01255; -.
DR SMR; Q01255; -.
DR STRING; 1288.SXYLSMQ121_0901; -.
DR eggNOG; COG1055; Bacteria.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015105; F:arsenite transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR CDD; cd01118; ArsB_permease; 1.
DR InterPro; IPR000802; Arsenical_pump_ArsB.
DR Pfam; PF02040; ArsB; 1.
DR PRINTS; PR00758; ARSENICPUMP.
DR TIGRFAMs; TIGR00935; 2a45; 1.
PE 3: Inferred from homology;
KW Arsenical resistance; Cell membrane; Membrane; Plasmid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..429
FT /note="Arsenical pump membrane protein"
FT /id="PRO_0000201479"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 429 AA; 46561 MW; 7157F73E4D093510 CRC64;
MTILAIVIFL LTLIFVIWQP KGLDIGITAL IGAVVAIITG VVSFSDVLEV TGIVWNATLT
FVAVILISLI LDEIGFFEWS AIHMVKASNG NGLKMFVFIM LLGAIVAAFF ANDGAALILT
PIVLAMVRNL GFNKKVIFPF IIASGFIADT TSLPLIVSNL VNIVSADYFD IGFIEYFSRM
IIPNIFSLIA SILVLWLYFR KSIPKTFNTE NLSDPKNVIK DPKLFKLSWI VLAILLVGYL
VSEFIQIPVS IIAGIIALIF VILARKSKAV HTKQVIKGAP WNIVVFSIGM YLVVFGLKNV
GITTILGDIL TNISSYGLFS SIMGMGFIAA FLSSIMNNMP TVLIDAIAIG QSSATGILKE
GMVYANVIGS DLGPKITPIG SLATLLWLHV LTQKGVKISW GTYFKTGIII TIPVLFVTLL
GLYLTLIIF