ID GSIC_ECOLI Reviewed; 306 AA.
AC P75798;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 161.
DE RecName: Full=Glutathione transport system permease protein GsiC {ECO:0000305};
GN Name=gsiC {ECO:0000303|PubMed:16109926}; Synonyms=yliC;
GN OrderedLocusNames=b0831, JW0815;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION IN GLUTATHIONE TRANSPORT, AND SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16109926; DOI=10.1128/jb.187.17.5861-5867.2005;
RA Suzuki H., Koyanagi T., Izuka S., Onishi A., Kumagai H.;
RT "The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel
RT glutathione importer with an ATP-binding cassette.";
RL J. Bacteriol. 187:5861-5867(2005).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP INTERACTION WITH GSIB.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=30515393; DOI=10.1155/2018/3429569;
RA Wang Z., Xia X., Zhang M., Fang J., Li Y., Zhang M.;
RT "Purification and characterization of glutathione binding protein GsiB from
RT Escherichia coli.";
RL Biomed. Res. Int. 2018:3429569-3429569(2018).
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:0000305|PubMed:16109926}.
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) (Probable). In the presence of glutathione, interacts with the
CC glutathione-binding protein GsiB (PubMed:30515393).
CC {ECO:0000269|PubMed:30515393, ECO:0000305|PubMed:16109926}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; 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; U00096; AAC73918.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35526.1; -; Genomic_DNA.
DR PIR; G64820; G64820.
DR RefSeq; NP_415352.1; NC_000913.3.
DR RefSeq; WP_000936043.1; NZ_STEB01000019.1.
DR AlphaFoldDB; P75798; -.
DR SMR; P75798; -.
DR BioGRID; 4259983; 14.
DR ComplexPortal; CPX-4325; Glutathione ABC transporter complex.
DR IntAct; P75798; 2.
DR STRING; 511145.b0831; -.
DR TCDB; 3.A.1.5.11; the atp-binding cassette (abc) superfamily.
DR PaxDb; 511145-b0831; -.
DR EnsemblBacteria; AAC73918; AAC73918; b0831.
DR GeneID; 75204704; -.
DR GeneID; 945460; -.
DR KEGG; ecj:JW0815; -.
DR KEGG; eco:b0831; -.
DR PATRIC; fig|1411691.4.peg.1447; -.
DR EchoBASE; EB3247; -.
DR eggNOG; COG0601; Bacteria.
DR HOGENOM; CLU_036879_0_0_6; -.
DR InParanoid; P75798; -.
DR OMA; ALAMYSM; -.
DR OrthoDB; 9805855at2; -.
DR PhylomeDB; P75798; -.
DR BioCyc; EcoCyc:YLIC-MONOMER; -.
DR BioCyc; MetaCyc:YLIC-MONOMER; -.
DR BRENDA; 7.4.2.10; 2026.
DR PRO; PR:P75798; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; NAS:ComplexPortal.
DR GO; GO:0016020; C:membrane; NAS:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; MetI-like; 1.
DR InterPro; IPR045621; BPD_transp_1_N.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR43163; DIPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN DPPB-RELATED; 1.
DR PANTHER; PTHR43163:SF5; GLUTATHIONE TRANSPORT SYSTEM PERMEASE PROTEIN GSIC; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF19300; BPD_transp_1_N; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
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_0000060261"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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:0000305"
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:0000305"
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:0000305"
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:0000305"
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:0000305"
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:0000269|PubMed:15919996"
FT DOMAIN 95..292
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 306 AA; 34066 MW; B74F4D9F2527AECE CRC64;
MLNYVIKRLL GLIPTLFIVS VLVFLFVHML PGDPARLIAG PEADAQVIEL VRQQLGLDQP
LYHQFWHYIS NAVQGDFGLS MVSRRPVADE IASRFMPTLW LTITSMVWAV IFGMAAGIIA
AVWRNRWPDR LSMTIAVSGI SFPAFALGML LIQVFSVELG WLPTVGADSW QHYILPSLTL
GAAVAAVMAR FTRASFVDVL SEDYMRTARA KGVSETWVVL KHGLRNAMIP VVTMMGLQFG
FLLGGSIVVE KVFNWPGLGR LLVDSVEMRD YPVIQAEILL FSLEFILINL VVDVLYAAIN
PAIRYK
//
