ID   GSIB_SHIBS              Reviewed;         512 AA.
AC   Q323W4;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Glutathione-binding protein GsiB {ECO:0000250|UniProtKB:P75797};
DE   Flags: Precursor;
GN   Name=gsiB {ECO:0000250|UniProtKB:P75797}; OrderedLocusNames=SBO_0720;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000036; ABB65394.1; -; Genomic_DNA.
DR   RefSeq; WP_000090142.1; NC_007613.1.
DR   AlphaFoldDB; Q323W4; -.
DR   SMR; Q323W4; -.
DR   EnsemblBacteria; ABB65394; ABB65394; SBO_0720.
DR   KEGG; sbo:SBO_0720; -.
DR   HOGENOM; CLU_017028_7_3_6; -.
DR   OMA; KESPWVP; -.
DR   Proteomes; UP000007067; 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; Signal; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..512
FT                   /note="Glutathione-binding protein GsiB"
FT                   /id="PRO_0000279982"
SQ   SEQUENCE   512 AA;  56442 MW;  F004CF54533E2653 CRC64;
     MARAVHRSGL VALGIATALM ASCAFAAKDV VVAVGSNFTT LDPYDANDTL SQAVAKSFYQ
     GLFGLDKEMK LKNVLAESYT VSDDGITYTV KLREGIKFQD GTDFNAAAVK ANLDRASDPA
     NHLKRYNLYK NIAKTEAIDP TTVKITLKQP FSAFINILVH PATAMISPAA LEKYGKEIGF
     HPVGTGPYEL DTWNQTDFVK VKKFAGYWQP GLPKLDSITW RPVADNNTRA AMLQTGEAQF
     AFPIPYEQAA 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