ARSB_STAAR
ID ARSB_STAAR Reviewed; 429 AA.
AC Q6GFT0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Arsenical pump membrane protein;
DE AltName: Full=Arsenic efflux pump protein;
GN Name=arsB; OrderedLocusNames=SAR1856;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAG40847.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX571856; CAG40847.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q6GFT0; -.
DR SMR; Q6GFT0; -.
DR KEGG; sar:SAR1856; -.
DR HOGENOM; CLU_043931_1_0_9; -.
DR OMA; SWGYYFK; -.
DR Proteomes; UP000000596; Chromosome.
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; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..429
FT /note="Arsenical pump membrane protein"
FT /id="PRO_0000201473"
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 99..119
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; 47042 MW; A48E4F6F977C3DCD CRC64;
MTTLATFIFL VTLLFVLWQP KGLDIGFTAL AGAFIAVITG VVSFSDVFEV TGIVWNATLT
FVSVILISLI LDKVGLFEWS AIHMLHASKG SGLKMFVYII LLGAVVAAFF ANDGAALILT
PIVLAMVKNI GFSKRAIFPF IIASGFIADT TSLPLIVSNL VNIISADYFN ISFSQYLSRM
IIPNLFSLLA SLLVLWLYFR KAIPKSFDAN HIKKPIDAIN DLKLFKISWI VLVILLFGYL
ISEFTKIPVS IFTGIIAFIF LILARKSNAV NIKQVIKGAP WNIVLFSIGM YIVVFGLRNA
GITLILAKIL EYISNYGLFS TILGMGFISA FLSSIMNNMP TVLIDAIAIG QSNVHGMLKE
GLIYANVIGS DLGPKITPIG SLATLLWLHV LTQKDVKISW GTYFKTGIII TIPVLFFTLL
GLYLTLILF