ID GSIB_ECOL6 Reviewed; 512 AA.
AC Q8CW88;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Glutathione-binding protein GsiB {ECO:0000250|UniProtKB:P75797};
DE Flags: Precursor;
GN Name=gsiB {ECO:0000250|UniProtKB:P75797}; OrderedLocusNames=c0915;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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=AAN79388.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN79388.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000090180.1; NZ_CP051263.1.
DR AlphaFoldDB; Q8CW88; -.
DR SMR; Q8CW88; -.
DR STRING; 199310.c0915; -.
DR KEGG; ecc:c0915; -.
DR eggNOG; COG0747; Bacteria.
DR HOGENOM; CLU_017028_7_3_6; -.
DR Proteomes; UP000001410; 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 CDD; cd08499; PBP2_Ylib_like; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
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:SF32; GLUTATHIONE-BINDING PROTEIN GSIB; 1.
DR PANTHER; PTHR30290; PERIPLASMIC BINDING COMPONENT OF ABC TRANSPORTER; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 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_0000279976"
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
//
