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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
 
 
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