ARSB_STAEQ
ID ARSB_STAEQ Reviewed; 430 AA.
AC Q5HRI3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Arsenical pump membrane protein;
DE AltName: Full=Arsenic efflux pump protein;
GN Name=arsB; OrderedLocusNames=SERP0210;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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}.
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DR EMBL; CP000029; AAW53574.1; -; Genomic_DNA.
DR RefSeq; WP_002445751.1; NC_002976.3.
DR AlphaFoldDB; Q5HRI3; -.
DR SMR; Q5HRI3; -.
DR STRING; 176279.SERP0210; -.
DR EnsemblBacteria; AAW53574; AAW53574; SERP0210.
DR KEGG; ser:SERP0210; -.
DR eggNOG; COG1055; Bacteria.
DR HOGENOM; CLU_043931_1_0_9; -.
DR OMA; SWGYYFK; -.
DR OrthoDB; 626718at2; -.
DR Proteomes; UP000000531; 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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..430
FT /note="Arsenical pump membrane protein"
FT /id="PRO_0000201478"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 430 AA; 47142 MW; B90DF03C597E6EA9 CRC64;
MTTVLAIVIF FITLTLIIWQ PKGLDIGISA IIGALLVIIT GVVNFTDILE VIGIVWNATL
TFVSVILISL ILDEIGFFEW SAIHMVKASN GHGLKMFIYI MILGALIAAF FANDGAALIL
TPIVLAMIRN LGFNNKLVFP FIIACGFIAD STSLPLVVSN LVNIVSADYF GIKFVEYLMR
MFIPNLFSLL ASILVLWFYF RKSIPKTFDI SSISEPKDAI RDTRLFKISW IILALLLIGY
LVSEFIHIPV SFITGAIAVI FILLARQSNV VHTKQVIKGA PWNIVIFSIG MYLVIFGLKN
VGMTLILADI LSSIAQHGLF SSIMGMGFVS AFLSAIMNNM PTVLIDAIAI DQSHAISSIK
EGMIYANVIG ADLGPKITPI GSLATLLWLH VLVQKGVKIS WGTYFKTGIV ITIPVLFFTL
LGLYLTLIIF