GSIC_SHIFL
ID GSIC_SHIFL Reviewed; 306 AA.
AC Q83S26; Q7C2E6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Glutathione transport system permease protein GsiC {ECO:0000250|UniProtKB:P75798};
GN Name=gsiC {ECO:0000250|UniProtKB:P75798}; OrderedLocusNames=SF0781, S0824;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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:P75798}.
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:P75798}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P75798}; 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; AE005674; AAN42415.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16291.1; -; Genomic_DNA.
DR RefSeq; NP_706708.1; NC_004337.2.
DR RefSeq; WP_000967687.1; NZ_WPGW01000058.1.
DR AlphaFoldDB; Q83S26; -.
DR SMR; Q83S26; -.
DR STRING; 198214.SF0781; -.
DR EnsemblBacteria; AAN42415; AAN42415; SF0781.
DR EnsemblBacteria; AAP16291; AAP16291; S0824.
DR GeneID; 1023769; -.
DR KEGG; sfl:SF0781; -.
DR KEGG; sft:NCTC1_00791; -.
DR KEGG; sfx:S0824; -.
DR PATRIC; fig|198214.7.peg.906; -.
DR HOGENOM; CLU_036879_0_0_6; -.
DR OMA; MQEDYMR; -.
DR OrthoDB; 1479518at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; IPR045621; BPD_transp_1_N.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF19300; BPD_transp_1_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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..306
FT /note="Glutathione transport system permease protein GsiC"
FT /id="PRO_0000279999"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 30..102
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 124..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 156..168
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 190..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 250..277
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 299..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 95..292
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 306 AA; 34150 MW; A5099EC0FBDF3BCD CRC64;
MLYYVIKRLL GLIPTLFIVS VLVFLFVHML PGDPARLIAG PEADAQVIEL VRQQLGLDQP
LYHQFWHYIS NAVQGDFGLS MVSRRPVADE IASRFMPTLW LTITSMVWAV IFGMAAGIIA
AVWRNRWPDR LSMTIAVSGI SFPAFALGMF LIQVFSVELG WLPTVGADSW QHYILPSLTL
GAAVAAVMAR FTRASFVDVL SEDYMRTARA KGVSETWVVL KHGLRNAMIP VVTMMGLQFG
FLLGGSIVVE KVFNWPGLGR LLVDSVEMRD YPVIQAEILL FSLEFILINL VVDVLYAAIN
PAIRYK
