GSIB_ECOLI
ID GSIB_ECOLI Reviewed; 512 AA.
AC P75797; Q9R7R5; Q9R7R7; Q9R7R8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Glutathione-binding protein GsiB {ECO:0000305};
DE Flags: Precursor;
GN Name=gsiB {ECO:0000303|PubMed:16109926}; Synonyms=yliB;
GN OrderedLocusNames=b0830, JW5111;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [5]
RP FUNCTION IN GLUTATHIONE TRANSPORT, AND SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16109926; DOI=10.1128/jb.187.17.5861-5867.2005;
RA Suzuki H., Koyanagi T., Izuka S., Onishi A., Kumagai H.;
RT "The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel
RT glutathione importer with an ATP-binding cassette.";
RL J. Bacteriol. 187:5861-5867(2005).
RN [6]
RP FUNCTION, INTERACTION WITH GSIC AND GSID, AND DOMAIN.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=30515393; DOI=10.1155/2018/3429569;
RA Wang Z., Xia X., Zhang M., Fang J., Li Y., Zhang M.;
RT "Purification and characterization of glutathione binding protein GsiB from
RT Escherichia coli.";
RL Biomed. Res. Int. 2018:3429569-3429569(2018).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS) OF 24-512.
RX PubMed=14649299; DOI=10.1023/a:1026177202925;
RA Abergel C., Coutard B., Byrne D., Chenivesse S., Claude J.-B.,
RA Deregnaucourt C., Fricaux T., Gianesini-Boutreux C., Jeudy S., Lebrun R.,
RA Maza C., Notredame C., Poirot O., Suhre K., Varagnol M., Claverie J.-M.;
RT "Structural genomics of highly conserved microbial genes of unknown
RT function in search of new antibacterial targets.";
RL J. Struct. Funct. Genomics 4:141-157(2003).
CC -!- FUNCTION: Part of the ABC transporter complex GsiABCD involved in
CC glutathione import (PubMed:16109926). Binds glutathione
CC (PubMed:30515393). {ECO:0000269|PubMed:16109926,
CC ECO:0000269|PubMed:30515393}.
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) (Probable). In the presence of glutathione, interacts with the
CC transmembrane proteins GsiC and GsiD (PubMed:30515393).
CC {ECO:0000269|PubMed:30515393, ECO:0000305|PubMed:16109926}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- DOMAIN: Glutathione binding may promote conformational change, from
CC inactive to active form. {ECO:0000269|PubMed:30515393}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC73917.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35525.2; -; Genomic_DNA.
DR PIR; F64820; F64820.
DR RefSeq; NP_415351.1; NC_000913.3.
DR RefSeq; WP_000090140.1; NZ_SSZK01000002.1.
DR PDB; 1UQW; X-ray; 2.72 A; A/B=24-512.
DR PDBsum; 1UQW; -.
DR AlphaFoldDB; P75797; -.
DR SMR; P75797; -.
DR BioGRID; 4259982; 40.
DR ComplexPortal; CPX-4325; Glutathione ABC transporter complex.
DR DIP; DIP-12697N; -.
DR IntAct; P75797; 2.
DR STRING; 511145.b0830; -.
DR TCDB; 3.A.1.5.11; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P75797; -.
DR jPOST; P75797; -.
DR PaxDb; P75797; -.
DR PRIDE; P75797; -.
DR EnsemblBacteria; AAC73917; AAC73917; b0830.
DR EnsemblBacteria; BAA35525; BAA35525; BAA35525.
DR GeneID; 945459; -.
DR KEGG; ecj:JW5111; -.
DR KEGG; eco:b0830; -.
DR PATRIC; fig|511145.12.peg.857; -.
DR EchoBASE; EB3246; -.
DR eggNOG; COG0747; Bacteria.
DR HOGENOM; CLU_017028_7_3_6; -.
DR InParanoid; P75797; -.
DR OMA; KESPWVP; -.
DR PhylomeDB; P75797; -.
DR BioCyc; EcoCyc:YLIB-MON; -.
DR BioCyc; MetaCyc:YLIB-MON; -.
DR BRENDA; 7.4.2.10; 2026.
DR EvolutionaryTrace; P75797; -.
DR PRO; PR:P75797; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0042938; P:dipeptide transport; IBA:GO_Central.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000031807"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1UQW"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 71..81
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1UQW"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1UQW"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:1UQW"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 258..273
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 295..303
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 347..354
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 376..383
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 385..391
FT /evidence="ECO:0007829|PDB:1UQW"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:1UQW"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 442..452
FT /evidence="ECO:0007829|PDB:1UQW"
FT HELIX 457..474
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 477..490
FT /evidence="ECO:0007829|PDB:1UQW"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:1UQW"
SQ SEQUENCE 512 AA; 56470 MW; F7552060CA4FBF86 CRC64;
MARAVHRSGL VALGIATALM ASCAFAAKDV VVAVGSNFTT LDPYDANDTL SQAVAKSFYQ
GLFGLDKEMK LKNVLAESYT VSDDGITYTV KLREGIKFQD GTDFNAAAVK ANLDRASDPA
NHLKRYNLYK NIAKTEAIDP TTVKITLKQP FSAFINILAH PATAMISPAA LEKYGKEIGF
YPVGTGPYEL 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
