ID   GSIA_ECOL6              Reviewed;         623 AA.
AC   Q8FJL0;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 113.
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=c0914;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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=AAN79387.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014075; AAN79387.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001304780.1; NC_004431.1.
DR   AlphaFoldDB; Q8FJL0; -.
DR   SMR; Q8FJL0; -.
DR   STRING; 199310.c0914; -.
DR   EnsemblBacteria; AAN79387; AAN79387; c0914.
DR   KEGG; ecc:c0914; -.
DR   eggNOG; COG4172; Bacteria.
DR   HOGENOM; CLU_000604_86_3_6; -.
DR   OMA; DPMTRLD; -.
DR   Proteomes; UP000001410; 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; Repeat; Translocase; Transport.
FT   CHAIN           1..623
FT                   /note="Glutathione import ATP-binding protein GsiA"
FT                   /id="PRO_0000280021"
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;  69176 MW;  5707C4ABEB65C3B3 CRC64;
     MPHSDELDAG DVLAVENLNI AFMQEQQKIA AVRNLSFSLQ RGETLAIVGE SGSGKSVTAL
     ALMRLLEQAG GLVQCDKMLL QRRSREVIEL SEQSAAQMRH VRGADMAMIF QEPMTSLNPV
     FAVGEQIAES IRLHQNASRE EAMVEAKRML DQVRIPEAQT ILSRYPHQLS GGMRQRVMIA
     MALSCRPAVL IADEPTTALD VTIQAQILQL IKVLQKEMSM GVIFITHDMG VVAEIADRVL
     VMYQGEAVET GSVEQIFHAP QHPYTRALLA AVPQLGAMKG LDYPRRFPLI SLEHPAKQEP
     PIEQKTVVDG EPVLRVRNLV TRFPLRSGLL NRVTREVHAV EKVSFDLWPG ETLSLVGESG
     SGKSTTGRAL LRLVESQGGE IIFNGQRIDT LSPCKLQALR RDIQFIFQDP YASLDPRQTI
     GDSIIEPLRV HGLLPGKEAA ARVAWLLERV GLLPEHAWRY PHEFSGGQRQ RICIARALAL
     NPKVIIADEA VSALDVSIRG QIINLLLDLQ RDFGIAYLFI SHDMAVVERI SHRVAVMYLG
     QIVEIGPRRA VFENPQHPYT RKLLAAVPVA EPSRQRPQRV LLSDDLPSNI HLRGEEVAAV
     SLQCVGPGHY VAQPQSEYAF MRR