ID   GSIA_SHIDS              Reviewed;         623 AA.
AC   Q32IB5;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 98.
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=SDY_0758;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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: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=ABB60942.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000034; ABB60942.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024259449.1; NC_007606.1.
DR   RefSeq; YP_402431.1; NC_007606.1.
DR   AlphaFoldDB; Q32IB5; -.
DR   SMR; Q32IB5; -.
DR   STRING; 300267.SDY_0758; -.
DR   EnsemblBacteria; ABB60942; ABB60942; SDY_0758.
DR   KEGG; sdy:SDY_0758; -.
DR   PATRIC; fig|300267.13.peg.872; -.
DR   HOGENOM; CLU_000604_86_2_6; -.
DR   Proteomes; UP000002716; 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_0000280028"
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;  69149 MW;  CE65AED9C9D1B4F8 CRC64;
     MPHSDELDAG NVLAVENLNI AFMQDQQKIA AVRNLSFSLQ RGETLAIVGE SGSGKSVTAL
     ALMRLLEQAG GLVQCDKMLL RRRSRDVIEL SEQSATQMRH VRGADMAMIF QEPMTSLNPV
     FTVGEQIAES IRLHQNASRE EAMVEAKRML DQVRIPEAQT ILSRYPHQLS GGMRQRVMIA
     MALSCRPAVL IADEPTTALD VTIQAQILQL IKVLQKEMSM GVIFITHDMG VVAEIADRVL
     VMYQGEAVET GTVEQIFHAP QHPYTRALLA AVPQLGAMKG LDYPRRFPLI SLEHPAKQAP
     PIEQKTVVDG EPVLRVRNLV TRFSLRSGLL NRVTREVHAV EKVSFDLWPG ETLSLVGESG
     SGKSTTGRAL LRLVESQGGE IIFNGQRIDT LSPGKLQALR RDIQFIFQDP YASLDPRQTI
     GDSIIEPLRV HGLLPGKDAV ARVAWLLERV GLLPEHAWRY PHEFSGGQRQ RICIARALAL
     NPKVIIADEA VSALDVSIRG QIINLLLDLQ RDFGIAYLFI SHDMAVVERI SHRVAVMYLG
     QIVEIGPRRA VFENPQHPYT RKLLAAVPVA EPSRQRPQRV LLSDDLPSNI HLRGEEVAAV
     SLQCVGPGHY VAQPQSEYAF MRR