GSIA_SALTI
ID GSIA_SALTI Reviewed; 623 AA.
AC Q8Z864; Q7C8T6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=STY0887, t2041;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD05294.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69653.1; -; Genomic_DNA.
DR RefSeq; NP_455382.1; NC_003198.1.
DR RefSeq; WP_001120605.1; NZ_UCTX01000006.1.
DR AlphaFoldDB; Q8Z864; -.
DR SMR; Q8Z864; -.
DR STRING; 220341.16502058; -.
DR EnsemblBacteria; AAO69653; AAO69653; t2041.
DR KEGG; stt:t2041; -.
DR KEGG; sty:STY0887; -.
DR PATRIC; fig|220341.7.peg.896; -.
DR eggNOG; COG4172; Bacteria.
DR HOGENOM; CLU_000604_86_2_6; -.
DR OMA; DPMTRLD; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000280025"
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; 69149 MW; 56CEFFBA7729028C CRC64;
MPHSDELDSR DVLSVSGLNI AFHHEGQQVD AVRNVSLRLK RGETLTIVGE 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
