GSIA_ECO57
ID GSIA_ECO57 Reviewed; 623 AA.
AC Q8X6W1; Q7AGA6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glutathione import ATP-binding protein GsiA {ECO:0000250|UniProtKB:P75796};
DE EC=7.4.2.10 {ECO:0000250|UniProtKB:P75796};
GN Name=gsiA {ECO:0000250|UniProtKB:P75796}; OrderedLocusNames=Z1053, ECs0908;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Part of the ABC transporter complex GsiABCD involved in
CC glutathione import. Responsible for energy coupling to the transport
CC system. {ECO:0000250|UniProtKB:P75796}.
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:0000250|UniProtKB:P75796};
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:P75796}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P75796}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P75796}.
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=AAG55203.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB34331.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG55203.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB34331.1; ALT_INIT; Genomic_DNA.
DR PIR; D90742; D90742.
DR PIR; G85592; G85592.
DR RefSeq; NP_308935.2; NC_002695.1.
DR RefSeq; WP_001301498.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X6W1; -.
DR SMR; Q8X6W1; -.
DR STRING; 155864.EDL933_0954; -.
DR EnsemblBacteria; AAG55203; AAG55203; Z1053.
DR EnsemblBacteria; BAB34331; BAB34331; ECs_0908.
DR GeneID; 917648; -.
DR KEGG; ece:Z1053; -.
DR KEGG; ecs:ECs_0908; -.
DR PATRIC; fig|386585.9.peg.1023; -.
DR eggNOG; COG4172; Bacteria.
DR HOGENOM; CLU_000604_86_2_6; -.
DR OMA; DPMTRLD; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
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_0000280019"
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; 69143 MW; C74DA3FA88AE39FD CRC64;
MPHSDELDAG NVLAVENLNI AFMQDQQKIA AVRNLSFSLQ RGETLAIVGE SGSGKSVTAL
ALMRLLEQAG GLVQCDKMLL RRRSRDVIEL SEQSAAQMRH 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 HGLLPGKEAV ARVAWLLERV GLLPEHAWRY PHEFSGGQRQ RICIARALAL
NPKVIIADEA VSALDVSIRG QIINLLLDLQ RDFGIAYLFI SHDMAVVERI SHRVAVMYLG
QIVEIGPRRA VFENPQHPYT RKLLAAVPVA EPSRQRPQRV LLSDDLPSNI HLRGEEVAAV
SLQCVGPGHY VAQPQSEYAF MRR
