ACR3_CORGL
ID ACR3_CORGL Reviewed; 370 AA.
AC Q8NQC8; Q6M576;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Arsenical-resistance protein Acr3;
GN Name=acr3; Synonyms=arsC2; OrderedLocusNames=Cgl1510, cg1705;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF CYS-129 AND CYS-141.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
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).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-72; CYS-129; ARG-210;
RP THR-241; GLU-305 AND GLU-332.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=22102279; DOI=10.1074/jbc.m111.263335;
RA Villadangos A.F., Fu H.L., Gil J.A., Messens J., Rosen B.P., Mateos L.M.;
RT "Efflux permease CgAcr3-1 of Corynebacterium glutamicum is an arsenite-
RT specific antiporter.";
RL J. Biol. Chem. 287:723-735(2012).
CC -!- FUNCTION: Catalyzes the proton motive force-dependent arsenite efflux
CC from the cell. Probably functions as an arsenite/H(+) antiporter. Does
CC not transport antimonite. {ECO:0000269|PubMed:19494117,
CC ECO:0000269|PubMed:22102279}.
CC -!- ACTIVITY REGULATION: Inhibited by carbonyl cyanide m-
CC chlorophenylhydrazone (CCCP). {ECO:0000269|PubMed:22102279}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB98903.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000036; BAB98903.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927152; CAF21519.1; -; Genomic_DNA.
DR RefSeq; NP_600726.2; NC_003450.3.
DR RefSeq; WP_011265757.1; NC_006958.1.
DR AlphaFoldDB; Q8NQC8; -.
DR SMR; Q8NQC8; -.
DR STRING; 196627.cg1705; -.
DR TCDB; 2.A.59.1.7; the arsenical resistance-3 (acr3) family.
DR DNASU; 1019483; -.
DR KEGG; cgb:cg1705; -.
DR KEGG; cgl:Cgl1510; -.
DR PATRIC; fig|196627.13.peg.1478; -.
DR eggNOG; COG0798; Bacteria.
DR HOGENOM; CLU_022869_0_0_11; -.
DR BioCyc; MetaCyc:G18NG-11093-MON; -.
DR Proteomes; UP000000582; 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..370
FT /note="Arsenical-resistance protein Acr3"
FT /id="PRO_0000430361"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 72
FT /note="K->A: Decrease in transport activity."
FT /evidence="ECO:0000269|PubMed:22102279"
FT MUTAGEN 129
FT /note="C->A,S: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:19494117,
FT ECO:0000269|PubMed:22102279"
FT MUTAGEN 141
FT /note="C->S: Does not affect transport activity."
FT /evidence="ECO:0000269|PubMed:19494117"
FT MUTAGEN 210
FT /note="R->A: Decrease in transport activity."
FT /evidence="ECO:0000269|PubMed:22102279"
FT MUTAGEN 241
FT /note="T->A: Does not affect transport activity."
FT /evidence="ECO:0000269|PubMed:22102279"
FT MUTAGEN 305
FT /note="E->A,D,F,K: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:22102279"
FT MUTAGEN 332
FT /note="E->A: Decrease in transport activity."
FT /evidence="ECO:0000269|PubMed:22102279"
SQ SEQUENCE 370 AA; 40011 MW; 34C49C31A9497AA7 CRC64;
MTNSTQTRAK PARISFLDKY IPLWIILAMA FGLFLGRSVS GLSGFLGAME VGGISLPIAL
GLLVMMYPPL AKVRYDKTKQ IATDKHLMGV SLILNWVVGP ALMFALAWLF LPDQPELRTG
LIIVGLARCI AMVLVWSDMS CGDREATAVL VAINSVFQVA MFGALGWFYL QVLPSWLGLP
TTTAQFSFWS IVTSVLVFLG IPLLAGVFSR IIGEKIKGRE WYEQKFLPAI SPFALIGLLY
TIVLLFSLQG DQIVSQPWAV VRLAIPLVIY FVGMFFISLI ASKLSGMNYA KSASVSFTAA
GNNFELAIAV SIGTFGATSA QAMAGTIGPL IEIPVLVGLV YAMLWLGPKL FPNDPTLPSS
ARSTSQIINS
