ID   GSIA_ECOUT              Reviewed;         623 AA.
AC   Q1RE96;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 87.
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=UTI89_C0832;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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=ABE06318.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000243; ABE06318.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001350597.1; NC_007946.1.
DR   AlphaFoldDB; Q1RE96; -.
DR   SMR; Q1RE96; -.
DR   EnsemblBacteria; ABE06318; ABE06318; UTI89_C0832.
DR   KEGG; eci:UTI89_C0832; -.
DR   HOGENOM; CLU_000604_86_2_6; -.
DR   OMA; DPMTRLD; -.
DR   Proteomes; UP000001952; 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_0000280018"
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;  69155 MW;  A7F6EFFAD0C6116A CRC64;
     MPHSDELDAG DVLAVENLNI AFMQEQHKIA AVRNLSFSLQ RGETLAIVGE SGSGKSVTAL
     ALMRLLEQAG GLVQCDKMLL QRRSREVIEL SEQSAAQMRH VRGADMAMIF QEPMTSLNPV
     FTVGEQIAES IRLHQNASRE EAMVEAKRML DQVRIPEAQT ILSRYPHQLS GGMRQRVMIA
     MALSCRPAVL IADEPTTALD VTIQAQILQL IKVLQKEMSM GVIFITHDMG VVAEIADRVL
     VMYQGEAVET GSVEQIFHAP QHPYTRALLA AVPQLGAMKG LDYPRRFPLI SLEHPAKQEP
     PIEQKTVVDG EPVLRVRNLV SRFPLRSGLL NRVTREVHAV EKVSFDLWPG ETLSLVGESG
     SGKSTTGRAL LRLVESQGGE IIFNGQRIDT LSPGKLQALR RDIQFIFQDP YASLDPRQTI
     GDSILEPLRV HGLLPGKEAA ARVAWLLERV GLLPEHAWRY PHEFSGGQRQ RICIARALAL
     NPKVIIADEA VSALDVSIRG QIINLLLDLQ RDFGIAYLFI SHDMAVVERI SHRVAVMYLG
     QIVEIGPRRA VFENPQHPYT RKLLAAVPVA EPSRQRPQRV LLSDDLPSNI HLRGEEVAAV
     SLQCVGPGHY VAQPQSEYAF MRR