YEHZ_ECOLI
ID YEHZ_ECOLI Reviewed; 305 AA.
AC P33362; Q2MAU8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glycine betaine-binding protein YehZ {ECO:0000305};
DE Flags: Precursor;
GN Name=yehZ; Synonyms=osmF; OrderedLocusNames=b2131, JW2119;
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 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
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 INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15251200; DOI=10.1016/j.femsle.2004.05.046;
RA Checroun C., Gutierrez C.;
RT "Sigma(s)-dependent regulation of yehZYXW, which encodes a putative
RT osmoprotectant ABC transporter of Escherichia coli.";
RL FEMS Microbiol. Lett. 236:221-226(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), AND FUNCTION IN GLYCINE BETAINE
RP UPTAKE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=26325238; DOI=10.1021/acs.biochem.5b00274;
RA Lang S., Cressatti M., Mendoza K.E., Coumoundouros C.N., Plater S.M.,
RA Culham D.E., Kimber M.S., Wood J.M.;
RT "YehZYXW of Escherichia coli is a low-affinity, non-osmoregulatory betaine-
RT specific ABC transporter.";
RL Biochemistry 54:5735-5747(2015).
CC -!- FUNCTION: Part of an ABC transporter complex involved in low-affinity
CC glycine betaine uptake. Binds glycine betaine with low affinity.
CC {ECO:0000269|PubMed:26325238}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (YehX),
CC two transmembrane proteins (YehW and YehY) and a solute-binding protein
CC (YehZ). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- INDUCTION: Expression is sigma S-dependent. Induced by both osmotic
CC shock and entry into stationary phase. {ECO:0000269|PubMed:15251200}.
CC -!- SIMILARITY: Belongs to the OsmX family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be part of an osmoprotectant uptake
CC system (PubMed:15251200). However, it was shown later that the complex
CC does not mediate osmotic stress protection (PubMed:26325238).
CC {ECO:0000305|PubMed:15251200, ECO:0000305|PubMed:26325238}.
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DR EMBL; U00007; AAA60494.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75192.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76608.1; -; Genomic_DNA.
DR PIR; B64981; B64981.
DR RefSeq; NP_416635.1; NC_000913.3.
DR RefSeq; WP_001130308.1; NZ_LN832404.1.
DR PDB; 4WEP; X-ray; 1.50 A; A/B=24-305.
DR PDBsum; 4WEP; -.
DR AlphaFoldDB; P33362; -.
DR SMR; P33362; -.
DR BioGRID; 4260450; 111.
DR ComplexPortal; CPX-4449; Low affinity betaine ABC transporter complex.
DR IntAct; P33362; 3.
DR STRING; 511145.b2131; -.
DR TCDB; 3.A.1.12.15; the atp-binding cassette (abc) superfamily.
DR jPOST; P33362; -.
DR PaxDb; P33362; -.
DR PRIDE; P33362; -.
DR EnsemblBacteria; AAC75192; AAC75192; b2131.
DR EnsemblBacteria; BAE76608; BAE76608; BAE76608.
DR GeneID; 946681; -.
DR KEGG; ecj:JW2119; -.
DR KEGG; eco:b2131; -.
DR PATRIC; fig|1411691.4.peg.113; -.
DR EchoBASE; EB1950; -.
DR eggNOG; COG1732; Bacteria.
DR HOGENOM; CLU_038355_1_1_6; -.
DR InParanoid; P33362; -.
DR OMA; KDPAWKN; -.
DR PhylomeDB; P33362; -.
DR BioCyc; EcoCyc:YEHZ-MON; -.
DR BioCyc; MetaCyc:YEHZ-MON; -.
DR PRO; PR:P33362; -.
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:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0015838; P:amino-acid betaine transport; IC:ComplexPortal.
DR GO; GO:0071474; P:cellular hyperosmotic response; IEP:EcoCyc.
DR GO; GO:0031460; P:glycine betaine transport; IDA:EcoCyc.
DR InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
DR Pfam; PF04069; OpuAC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Periplasm; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..305
FT /note="Glycine betaine-binding protein YehZ"
FT /id="PRO_0000013871"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 35..50
FT /evidence="ECO:0007829|PDB:4WEP"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:4WEP"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4WEP"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:4WEP"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4WEP"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:4WEP"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4WEP"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:4WEP"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:4WEP"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:4WEP"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:4WEP"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:4WEP"
SQ SEQUENCE 305 AA; 32609 MW; 7823749E8575B784 CRC64;
MPLLKLWAGS LVMLAAVSLP LQAASPVKVG SKIDTEGALL GNIILQVLES HGVPTVNKVQ
LGTTPVVRGA ITSGELDIYP EYTGNGAFFF KDENDAAWKN AQQGYEKVKK LDSEHNKLIW
LTPAPANNTW TIAVRQDVAE KNKLTSLADL SRYLQEGGTF KLAASAEFIE RADALPAFEK
AYGFKLGQDQ LLSLAGGDTA VTIKAAAQQT SGVNAAMAYG TDGPVAALGL QTLSDPQGVQ
PIYAPAPVVR ESVLREYPQM AQWLQPVFAS LDAKTLQQLN ASIAVEGLDA KKVAADYLKQ
KGWTK
