ID   GSIA_SALCH              Reviewed;         623 AA.
AC   Q57RB2;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 97.
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=SCH_0843;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(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=AAX64749.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017220; AAX64749.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001120603.1; NC_006905.1.
DR   AlphaFoldDB; Q57RB2; -.
DR   SMR; Q57RB2; -.
DR   EnsemblBacteria; AAX64749; AAX64749; SCH_0843.
DR   KEGG; sec:SCH_0843; -.
DR   HOGENOM; CLU_000604_86_2_6; -.
DR   Proteomes; UP000000538; 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_0000280023"
FT   DOMAIN          15..269
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          325..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;  69218 MW;  B7DA7DA38DDB1B76 CRC64;
     MPHSDELDSR DVLSVSGLNI AFHHEGQQVD AVRNVSLRLK RGETLAIVGE SGSGKSVTAL
     ALMRLIEQSG ANVRCGEMLL RRRNRQVIEL SEQSDAQMRR VRGADIAMIF QEPMTSLNPV
     FTVGEQIAES IRLHQRASHE EALAEAKRML DQVRIPESQA ILSRYPHQLS GGMRQRVMIA
     MALSCRPAVL IADEPTTALD VTIQAQILQL IKVLQQEMSM GVIFITHDMG VVADIADRVL
     VMYQGEAVET GSVEQIFHAP THPYTQTLLA AVPQLGAMRG HSLPRRFPLI SADEPALYES
     QIEQDTVVEG EPILQVRGLV TRFPLRSGLF NRVTREVHAV ENISFDLWPG ETLSLVGESG
     SGKSTTGRAL LRLVESRQGE IIFNGQRIDT LSAGKLQPLR RDIQCIFQDP YASLDPRQTV
     GYSIMEPLRI HGLGQGDAAA KRVAWLLERV GLRPEHAWRY PHEFSGGQRQ RICIARALAL
     NPKVIIADEA VSALDVSVRG QIINLLLDLQ REMGIAYLFI SHDMAVVERI SHRVAVMYLG
     QIVEMGPRRA VFENPQHPYT RKLMAAVPVA DPSRHRPRRV LLSDDIPSNI HKRGEETPAV
     SLQLVGPGHY VARPLQDNAL SRL