GSIA_ECOLI
ID GSIA_ECOLI Reviewed; 623 AA.
AC P75796; Q9R3H8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Glutathione import ATP-binding protein GsiA {ECO:0000305};
DE EC=7.4.2.10 {ECO:0000269|PubMed:16109926};
GN Name=gsiA {ECO:0000303|PubMed:16109926}; Synonyms=yliA;
GN OrderedLocusNames=b0829, JW5897;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP 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).
CC -!- FUNCTION: Part of the ABC transporter complex GsiABCD involved in
CC glutathione import. Responsible for energy coupling to the transport
CC system. {ECO:0000269|PubMed:16109926}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glutathione(out) + H2O = ADP + glutathione(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:29791, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; EC=7.4.2.10;
CC Evidence={ECO:0000269|PubMed:16109926};
CC -!- ACTIVITY REGULATION: Inhibited by verapamil but not by carbonyl cyanide
CC m-chlorophenylhydrazone (CCCP). {ECO:0000269|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). {ECO:0000305|PubMed:16109926}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Glutathione
CC importer (TC 3.A.1.5.11) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA35517.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC73916.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35517.2; ALT_INIT; Genomic_DNA.
DR PIR; E64820; E64820.
DR RefSeq; NP_415350.2; NC_000913.3.
DR RefSeq; WP_001301279.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P75796; -.
DR SMR; P75796; -.
DR BioGRID; 4259981; 709.
DR ComplexPortal; CPX-4325; Glutathione ABC transporter complex.
DR STRING; 511145.b0829; -.
DR TCDB; 3.A.1.5.11; the atp-binding cassette (abc) superfamily.
DR jPOST; P75796; -.
DR PaxDb; P75796; -.
DR PRIDE; P75796; -.
DR EnsemblBacteria; AAC73916; AAC73916; b0829.
DR EnsemblBacteria; BAA35517; BAA35517; BAA35517.
DR GeneID; 945457; -.
DR KEGG; ecj:JW5897; -.
DR KEGG; eco:b0829; -.
DR PATRIC; fig|1411691.4.peg.1449; -.
DR EchoBASE; EB3245; -.
DR eggNOG; COG4172; Bacteria.
DR HOGENOM; CLU_000604_86_2_6; -.
DR InParanoid; P75796; -.
DR OMA; DPMTRLD; -.
DR PhylomeDB; P75796; -.
DR BioCyc; EcoCyc:YLIA-MON; -.
DR BioCyc; MetaCyc:YLIA-MON; -.
DR BRENDA; 7.4.2.10; 2026.
DR PRO; PR:P75796; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0015833; P:peptide transport; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR013563; Oligopep_ABC_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF08352; oligo_HPY; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Translocase; Transport.
FT CHAIN 1..623
FT /note="Glutathione import ATP-binding protein GsiA"
FT /id="PRO_0000093195"
FT DOMAIN 15..269
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 314..564
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 357..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 623 AA; 69114 MW; A11DB7EC235F9F76 CRC64;
MPHSDELDAG NVLAVENLNI AFMQDQQKIA AVRNLSFSLQ RGETLAIVGE SGSGKSVTAL
ALMRLLEQAG GLVQCDKMLL QRRSREVIEL SEQNAAQMRH VRGADMAMIF QEPMTSLNPV
FTVGEQIAES IRLHQNASRE EAMVEAKRML DQVRIPEAQT ILSRYPHQLS GGMRQRVMIA
MALSCRPAVL IADEPTTALD VTIQAQILQL IKVLQKEMSM GVIFITHDMG VVAEIADRVL
VMYQGEAVET GTVEQIFHAP QHPYTRALLA AVPQLGAMKG LDYPRRFPLI SLEHPAKQAP
PIEQKTVVDG EPVLRVRNLV TRFPLRSGLL NRVTREVHAV EKVSFDLWPG ETLSLVGESG
SGKSTTGRAL LRLVESQGGE IIFNGQRIDT LSPGKLQALR RDIQFIFQDP YASLDPRQTI
GDSIIEPLRV HGLLPGKDAA ARVAWLLERV GLLPEHAWRY PHEFSGGQRQ RICIARALAL
NPKVIIADEA VSALDVSIRG QIINLLLDLQ RDFGIAYLFI SHDMAVVERI SHRVAVMYLG
QIVEIGPRRA VFENPQHPYT RKLLAAVPVA EPSRQRPQRV LLSDDLPSNI HLRGEEVAAV
SLQCVGPGHY VAQPQSEYAF MRR
