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AQPS_RHIME
ID   AQPS_RHIME              Reviewed;         233 AA.
AC   Q92R43;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Aquaglyceroporin AqpS {ECO:0000303|PubMed:16199569};
GN   Name=aqpS {ECO:0000303|PubMed:16199569};
GN   ORFNames=SMc02648 {ECO:0000312|EMBL:CAC45655.1};
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=1021;
RX   PubMed=16199569; DOI=10.1128/jb.187.20.6991-6997.2005;
RA   Yang H.C., Cheng J., Finan T.M., Rosen B.P., Bhattacharjee H.;
RT   "Novel pathway for arsenic detoxification in the legume symbiont
RT   Sinorhizobium meliloti.";
RL   J. Bacteriol. 187:6991-6997(2005).
RN   [4]
RP   FUNCTION IN TRANSPORT OF METHYLARSENICALS, AND MUTAGENESIS OF THR-49 AND
RP   VAL-177.
RC   STRAIN=1021;
RX   PubMed=33418223; DOI=10.1016/j.chemosphere.2020.129379;
RA   Chen J., Nadar V.S., Rosen B.P.;
RT   "Aquaglyceroporin AqpS from Sinorhizobium meliloti conducts both trivalent
RT   and pentavalent methylarsenicals.";
RL   Chemosphere 270:129379-129379(2021).
CC   -!- FUNCTION: Involved in resistance to arsenic. Facilitates efflux of
CC       arsenite [As(III)]. Arsenate [As(V)] enters the cell through phosphate
CC       transport systems and is reduced to arsenite by the arsenate reductase
CC       ArsC. Internally generated arsenite flows out of the cell by downhill
CC       movement through AqpS (PubMed:16199569). Can also transport the highly
CC       toxic methylarsenite [MAs(III)] and the relatively non-toxic
CC       methylarsenate [MAs(V)]. May be a component of an methylarsenite
CC       resistance pathway in which methylarsenite enters cells via AqpS, is
CC       oxidized by ArsH to methylarsenate, which exits the cells via AqpS.
CC       This pathway may confer a selective advantage for R.melliloti to grow
CC       in the presence of environmental methylarsenicals (PubMed:33418223).
CC       {ECO:0000269|PubMed:16199569, ECO:0000269|PubMed:33418223}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC       membrane-spanning domains and a pore-forming loop with the signature
CC       motif Asn-Pro-Ala (NPA). {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene results in increased
CC       tolerance to arsenite but not arsenate. Does not affect sensitivity to
CC       antimonate [Sb(V)]. {ECO:0000269|PubMed:16199569}.
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. NIP (TC
CC       1.A.8.12) subfamily. {ECO:0000305}.
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DR   EMBL; AL591688; CAC45655.1; -; Genomic_DNA.
DR   RefSeq; NP_385182.1; NC_003047.1.
DR   RefSeq; WP_010969025.1; NC_003047.1.
DR   AlphaFoldDB; Q92R43; -.
DR   SMR; Q92R43; -.
DR   STRING; 266834.SMc02648; -.
DR   TCDB; 1.A.8.12.10; the major intrinsic protein (mip) family.
DR   EnsemblBacteria; CAC45655; CAC45655; SMc02648.
DR   GeneID; 61602536; -.
DR   KEGG; sme:SMc02648; -.
DR   PATRIC; fig|266834.11.peg.2482; -.
DR   eggNOG; COG0580; Bacteria.
DR   HOGENOM; CLU_020019_8_0_5; -.
DR   OMA; TGGAQWF; -.
DR   BioCyc; MetaCyc:MON-21671; -.
DR   Proteomes; UP000001976; 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:0015267; F:channel activity; IEA:InterPro.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   PANTHER; PTHR45724; PTHR45724; 1.
DR   Pfam; PF00230; MIP; 2.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
PE   1: Evidence at protein level;
KW   Arsenical resistance; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..233
FT                   /note="Aquaglyceroporin AqpS"
FT                   /id="PRO_0000453039"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           69..71
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           174..176
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         49
FT                   /note="T->F,W: Increases uptake of both methylarsenite and
FT                   methylarsenate and exhibits higher sensitivity to
FT                   methylarsenite."
FT                   /evidence="ECO:0000269|PubMed:33418223"
FT   MUTAGEN         177
FT                   /note="V->I: Decreases methylarsenite transport activity
FT                   and results in higher resistance to methylarsenite. Slight
FT                   decrease in methylarsenate transport activity."
FT                   /evidence="ECO:0000269|PubMed:33418223"
FT   MUTAGEN         177
FT                   /note="V->R: Increases methylarsenite transport activity,
FT                   leading to lower resistance to methylarsenite. Nearly
FT                   complete loss of methylarsenate transport activity."
FT                   /evidence="ECO:0000269|PubMed:33418223"
SQ   SEQUENCE   233 AA;  24301 MW;  ABAD5ACF96C95655 CRC64;
     MQEFDLTRRC VAEALGTGLL VAAVVGSGIM ADALTADDAL ALVANTIATG AILVVLVTIL
     GPLSGAHFNP AVSLVFALSG RLTRRDCAAY VIAQVAGAIA GTALAHLMFD LPPLDMSMKV
     RTGPAQWLSE GVAAFGLVAT ILAGIRFHRE AVPWLVGLYI TAAYWFTAST SFANPAVALA
     RSFTNTFSGI RPGDLPGFVI AELLGAVCAL ALMRWLLQPA RPIIRQTSPE TAP
 
 
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