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GSID_ECOUT
ID   GSID_ECOUT              Reviewed;         303 AA.
AC   Q1RE93;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Glutathione transport system permease protein GsiD {ECO:0000250|UniProtKB:P75799};
GN   Name=gsiD {ECO:0000250|UniProtKB:P75799}; OrderedLocusNames=UTI89_C0835;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex GsiABCD involved in
CC       glutathione import. Probably responsible for the translocation of the
CC       substrate across the membrane. {ECO:0000250|UniProtKB:P75799}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GsiA),
CC       two transmembrane proteins (GsiC and GsiD) and a solute-binding protein
CC       (GsiB). {ECO:0000250|UniProtKB:P75799}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P75799}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; CP000243; ABE06321.1; -; Genomic_DNA.
DR   RefSeq; WP_001236052.1; NC_007946.1.
DR   AlphaFoldDB; Q1RE93; -.
DR   EnsemblBacteria; ABE06321; ABE06321; UTI89_C0835.
DR   KEGG; eci:UTI89_C0835; -.
DR   HOGENOM; CLU_028518_1_1_6; -.
DR   OMA; RAWWVVS; -.
DR   Proteomes; UP000001952; 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:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR025966; OppC_N.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF12911; OppC_N; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..303
FT                   /note="Glutathione transport system permease protein GsiD"
FT                   /id="PRO_0000280006"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          101..290
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   303 AA;  33226 MW;  6272C580B5D379E0 CRC64;
     MRLFNWRRQA VLNAMPLVKP DQVRTPWHEF WRRFRRQHMA MTAALFVILL IVVAIFARWI
     APYDAENYFD YDNLNNGPSL QHWFGVDSLG RDIFSRVLVG AQISLAAGVF AVFIGAAIGT
     LLGLLAGYYE GWWDRLSMRI CDVLFAFPGI LLAIAVVAVL GSGIANVIIA VAIFSIPAFA
     RLVRGNTLVL KQQTFIESAR SIGASDMTIL LRHILPGTVS SIVVFFTMRI GTSIISAASL
     SFLGLGAQPP TPEWGAMLNE ARADMVIAPH VAVFPALAIF LTVLAFNLLG DGLRDALDPK
     IKG
 
 
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