ID   GSIB_SALCH              Reviewed;         512 AA.
AC   Q57RB1;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Glutathione-binding protein GsiB {ECO:0000250|UniProtKB:P75797};
DE   Flags: Precursor;
GN   Name=gsiB {ECO:0000250|UniProtKB:P75797}; OrderedLocusNames=SCH_0844;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(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}.
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DR   EMBL; AE017220; AAX64750.1; -; Genomic_DNA.
DR   RefSeq; WP_000191437.1; NC_006905.1.
DR   AlphaFoldDB; Q57RB1; -.
DR   SMR; Q57RB1; -.
DR   EnsemblBacteria; AAX64750; AAX64750; SCH_0844.
DR   KEGG; sec:SCH_0844; -.
DR   HOGENOM; CLU_017028_7_3_6; -.
DR   OMA; KESPWVP; -.
DR   Proteomes; UP000000538; 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_0000279978"
SQ   SEQUENCE   512 AA;  56580 MW;  DA9E1124D2D8D134 CRC64;
     MTQFITHKWL AALGLASSIA AFPALAAKDV VVAVGSNFTT LDPYDANDTL SQAVAKSFYQ
     GLFGLDKDMK VKNVLAEGYT VSDDGLTYTI TLRRGVKFQD GADFNAAAVK ANLDRASNPD
     NHLKRYNLYK NIAKTEVVDP ATVKITLKQP FSAFINILAH PATAMISPQA LEKYGKDIGF
     HPVGTGPYQL ETWNQTDFVK VKKFAGYWQQ GLPKLDSITW RPVTDNNTRA AMLQTGEAQF
     AFPIPYEQAA LLAKNKNLEL VASPSIMQRY ISMNVTQKPF DNPKVREALN YAINRQALVK
     VAFAGYATPA TGVVPPSIAY AQSYQPWPYD PAKARELLKE AGYPDGFSTT LWSSHNHSTA
     QKVLQFTQQQ LAQIGIKARI TAMDAGQRAA EVEGKGQKES GVRMFYTGWS ASTGEADWAL
     SPLFASQNWP PTQFNTAFYS NKQVDSDLAA ALKTNDPQEK TRLYKEAQDI IWKESPWIPL
     VVEKLVSAHS KNLTGFWIMP DTGFSFDDAD LK