ID   GSIA_SALTY              Reviewed;         623 AA.
AC   Q8ZQM4;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=STM0848;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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}.
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DR   EMBL; AE006468; AAL19784.1; -; Genomic_DNA.
DR   RefSeq; NP_459825.1; NC_003197.2.
DR   RefSeq; WP_001120598.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZQM4; -.
DR   STRING; 99287.STM0848; -.
DR   PaxDb; Q8ZQM4; -.
DR   EnsemblBacteria; AAL19784; AAL19784; STM0848.
DR   GeneID; 1252367; -.
DR   KEGG; stm:STM0848; -.
DR   PATRIC; fig|99287.12.peg.885; -.
DR   HOGENOM; CLU_000604_86_2_6; -.
DR   OMA; DPMTRLD; -.
DR   PhylomeDB; Q8ZQM4; -.
DR   BioCyc; SENT99287:STM0848-MON; -.
DR   BRENDA; 7.4.2.10; 5542.
DR   Proteomes; UP000001014; 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_0000280026"
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;  69119 MW;  17CB6CB29CCA0A62 CRC64;
     MPHSDELDSR DVLSVSGLNI AFHHEGQQVD AVRNVSLRLK RGETLAIVGE SGSGKSVTAL
     ALMRLIEQSG ANVRCGEMLL RRRNRQVIEL SEQSDAQMRR VRGADIAMIF QEPMTSLNPV
     FTVGEQIAES IRLHQGASHE 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