GSIA_SHIFL
ID GSIA_SHIFL Reviewed; 623 AA.
AC Q83LT3; Q7UD85;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 5.
DT 03-AUG-2022, entry version 133.
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=SF0779, S0822;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN42413.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP16289.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN42413.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP16289.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_706706.2; NC_004337.2.
DR RefSeq; WP_001120569.1; NZ_WPGW01000058.1.
DR AlphaFoldDB; Q83LT3; -.
DR SMR; Q83LT3; -.
DR STRING; 198214.SF0779; -.
DR EnsemblBacteria; AAN42413; AAN42413; SF0779.
DR EnsemblBacteria; AAP16289; AAP16289; S0822.
DR GeneID; 1023721; -.
DR GeneID; 58389749; -.
DR KEGG; sfl:SF0779; -.
DR KEGG; sfx:S0822; -.
DR PATRIC; fig|198214.7.peg.904; -.
DR HOGENOM; CLU_000604_86_2_6; -.
DR OrthoDB; 1303270at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000280029"
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; 69086 MW; 6B51E8B1AC93A016 CRC64;
MPHSDELDAG NVLAVENLNI AFMQDQQKIA AVRNLSFSLQ RGETLAIVGE SGSGKSVTAL
ALMRLLEQAG GLVQCDKMLL RRRSRDVIEL SEQSAAQMRH VRGADMAMIF QEPMTSLNPV
FTVGEQIAES IRLHQNASRE EAMVEAKRML DQVRIPEAQT ILSRYSHQLS GGMRQRVMIA
MALSCRPAVL IADEPTTALD VTIQAQILQL IKVLQKEMSM GVIFITHDMG VVAEIADRVL
VMYQGEAVET GTVEQIFHAP QHPYTRALLA AVPQLGAMKG LDYPRRFPLI SLEHPAKQEP
PIEQKTVVDG EPVLRVRNLV TRFPLRSGLL NRVTREVHAV EKVSFDLWPG ETLSLVGESG
SGKSTTGRAL LRLVESQGGE IIFNGQRIDT LSPGKLQALR RDIQFIFQDP YASLDPRQTI
GDSIIEPLRV HGLLPGKDAA ARVAWLLERV GLLPEHAWRY PHEFSGGQRQ RICIARALAL
NPKVIIADEA VSALDVSIRG QIINLLLDLQ RDFGIAYLFI SHDMAVVERI SHRVAVMYLG
QIVEIGSRCA VFENPQHPYT RKLLAAVPVA EPSRQRPQRV LLSDDLPSNI HLRGEEVAAV
SLQCVGPGHY VAQPQSEYAF MRR
