ACR3_ALKMQ
ID ACR3_ALKMQ Reviewed; 357 AA.
AC A6TP80;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Arsenical-resistance protein Acr3;
GN Name=acr3; OrderedLocusNames=Amet_1828;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF CYS-27; CYS-91
RP AND CYS-138.
RC STRAIN=QYMF;
RX PubMed=19494117; DOI=10.1074/jbc.m109.011882;
RA Fu H.L., Meng Y., Ordonez E., Villadangos A.F., Bhattacharjee H., Gil J.A.,
RA Mateos L.M., Rosen B.P.;
RT "Properties of arsenite efflux permeases (Acr3) from Alkaliphilus
RT metalliredigens and Corynebacterium glutamicum.";
RL J. Biol. Chem. 284:19887-19895(2009).
CC -!- FUNCTION: Catalyzes arsenite efflux from the cell.
CC {ECO:0000269|PubMed:19494117}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19494117};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19494117}.
CC -!- SIMILARITY: Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59)
CC family. {ECO:0000305}.
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DR EMBL; CP000724; ABR47998.1; -; Genomic_DNA.
DR RefSeq; WP_012063033.1; NC_009633.1.
DR AlphaFoldDB; A6TP80; -.
DR SMR; A6TP80; -.
DR STRING; 293826.Amet_1828; -.
DR TCDB; 2.A.59.1.5; the arsenical resistance-3 (acr3) family.
DR EnsemblBacteria; ABR47998; ABR47998; Amet_1828.
DR KEGG; amt:Amet_1828; -.
DR eggNOG; COG0798; Bacteria.
DR HOGENOM; CLU_022869_0_2_9; -.
DR OMA; YAQINLP; -.
DR OrthoDB; 1493959at2; -.
DR Proteomes; UP000001572; 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:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0015103; F:inorganic anion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
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 PANTHER; PTHR43057; PTHR43057; 1.
DR Pfam; PF01758; SBF; 1.
DR PIRSF; PIRSF005508; Acr3; 1.
DR TIGRFAMs; TIGR00832; acr3; 1.
PE 1: Evidence at protein level;
KW Arsenical resistance; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..357
FT /note="Arsenical-resistance protein Acr3"
FT /id="PRO_0000430360"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..49
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..319
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 27
FT /note="C->S: Decrease in transport activity."
FT /evidence="ECO:0000269|PubMed:19494117"
FT MUTAGEN 91
FT /note="C->S: Does not affect transport activity."
FT /evidence="ECO:0000269|PubMed:19494117"
FT MUTAGEN 138
FT /note="C->A,S: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:19494117"
SQ SEQUENCE 357 AA; 39433 MW; F1CFB92D665766B8 CRC64;
MGNENVVHEG KGIGFFERYL TVWVAACIIV GVAIGQLLPA VPETLSRWEY AQVSIPVAIL
IWLMIYPMML KIDFTSIVEA TKKPKGIIVT CVTNWLIKPF TMYLIAAFFF KIVFQNLIPE
SLANDYLAGA VLLGAAPCTA MVFVWSHLTK GDPAYTLVQV AVNNIILLFA FTPIVAILLG
ITDVIVPYDT LFLSVVLFIV IPLVGGYLSR KYIVQSKGIE YFENVFLKKF DNVTIVGLLL
TLIIIFTFQA EVILSNPLHV LLIAVPLTIQ TFFIFFLAYG WSKAWKLPHN VASPAGMIGA
SNFFELAVAV AITLFGLNSG ATLATVVGVL VEVPVMLTLV KISNRTRHWF PEVAREN
