ID   GSIB_ECOK1              Reviewed;         512 AA.
AC   A1A968; A1A969;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Glutathione-binding protein GsiB {ECO:0000250|UniProtKB:P75797};
DE   Flags: Precursor;
GN   Name=gsiB {ECO:0000250|UniProtKB:P75797};
GN   OrderedLocusNames=Ecok1_07140/Ecok1_07150;
GN   ORFNames=APECO1_12632/APECO1_1263;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ00208.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
CC       Sequence=ABJ00209.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR   EMBL; CP000468; ABJ00208.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP000468; ABJ00209.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; WP_000090180.1; NZ_CADILS010000017.1.
DR   AlphaFoldDB; A1A968; -.
DR   SMR; A1A968; -.
DR   EnsemblBacteria; ABJ00208; ABJ00208; APECO1_12632.
DR   EnsemblBacteria; ABJ00209; ABJ00209; APECO1_1263.
DR   KEGG; ecv:APECO1_1263; -.
DR   KEGG; ecv:APECO1_12632; -.
DR   HOGENOM; CLU_743432_0_0_6; -.
DR   Proteomes; UP000008216; 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_0000279975"
SQ   SEQUENCE   512 AA;  56428 MW;  ABECB713B65F5694 CRC64;
     MARAVHRSGL VALGIATALM ASCAFAAKEV VVAVGSNFTT LDPYDANDTL SQAVAKSFYQ
     GLFGLDKEMK LKNVLAESYT VSDDGLTYTV KLREGIKFQD GTDFNAAAVK ANLDRASDPA
     NHLKRYNLYK NIAKTEAIDP TTVKITLKQP FSAFINILAH 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