ID   GSIB_SHIFL              Reviewed;         512 AA.
AC   Q821B3; Q7UD84;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 4.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Glutathione-binding protein GsiB {ECO:0000250|UniProtKB:P75797};
DE   Flags: Precursor;
GN   Name=gsiB {ECO:0000250|UniProtKB:P75797}; OrderedLocusNames=SF0780, S0823;
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. Binds glutathione. {ECO:0000250|UniProtKB:P75797}.
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:P75797}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P75797}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC       {ECO:0000305}.
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DR   EMBL; AE005674; AAN42414.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16290.1; -; Genomic_DNA.
DR   RefSeq; NP_706707.2; NC_004337.2.
DR   RefSeq; WP_000090147.1; NZ_WPGW01000058.1.
DR   AlphaFoldDB; Q821B3; -.
DR   SMR; Q821B3; -.
DR   STRING; 198214.SF0780; -.
DR   EnsemblBacteria; AAN42414; AAN42414; SF0780.
DR   EnsemblBacteria; AAP16290; AAP16290; S0823.
DR   GeneID; 1026150; -.
DR   KEGG; sfl:SF0780; -.
DR   KEGG; sfx:S0823; -.
DR   PATRIC; fig|198214.7.peg.905; -.
DR   HOGENOM; CLU_017028_7_3_6; -.
DR   OMA; KESPWVP; -.
DR   OrthoDB; 162819at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR030678; Peptide/Ni-bd.
DR   InterPro; IPR039424; SBP_5.
DR   InterPro; IPR023765; SBP_5_CS.
DR   InterPro; IPR000914; SBP_5_dom.
DR   PANTHER; PTHR30290; PTHR30290; 1.
DR   Pfam; PF00496; SBP_bac_5; 1.
DR   PIRSF; PIRSF002741; MppA; 1.
DR   PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE   3: Inferred from homology;
KW   Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..512
FT                   /note="Glutathione-binding protein GsiB"
FT                   /id="PRO_0000279984"
SQ   SEQUENCE   512 AA;  56502 MW;  805A1EB84471E24B CRC64;
     MARAVHRSGL VALGIATALM ASCAFAAKDV VVAVGSNFTT LDPYDANDTL SQAVAKSFYQ
     GLFGLDKEMK LKNVLAESYT VSDDGITYTV KLREGIKFQD GTDFNAVAVK ANLDRASDPA
     NHLKRYNLYK NIAKTEAIDP TTVKITLKQP FSAFINILAH PATAMISPTA LEKYGKEIGF
     HPVGTGPYEL DTWNQTDFVK VKKFAGYWQP GLPKLDSITW RPVADNNTRA AMLQTGEAQF
     AFPIPYEQAT LLEKNKNIEL MASPSIMQRY ISMNVTQKPF DNPKVREALN YAINRPALVK
     VAFAGYATPA TGVVPPSIAY AQSYKPWPYD PVKARELLKE AGYPNGFSTT LWSSHNHSTA
     QKVLQFTQQQ LAQVGIKAQV TAMDAGQRAA EVEGKGQKES GVRMFYTGWS ASTGEADWAL
     SPLFASQNWP PTLFNTAFYS NKQVDDFLAQ ALKTNDPAEK TRLYKAAQDI IWQESPWIPL
     VVEKLVSAHS KNLTGFWIMP DTGFSFEDAD LQ