YEHW_ECOLI
ID YEHW_ECOLI Reviewed; 243 AA.
AC P33359; Q2MAV1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Glycine betaine uptake system permease protein YehW {ECO:0000305};
GN Name=yehW; OrderedLocusNames=b2128, JW2116;
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 TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP FUNCTION IN GLYCINE BETAINE 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. Probably responsible for the translocation of
CC the substrate across the membrane. {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: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
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 binding-protein-dependent transport system
CC permease family. CysTW subfamily. {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; AAA60491.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75189.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76605.1; -; Genomic_DNA.
DR PIR; G64980; G64980.
DR RefSeq; NP_416632.1; NC_000913.3.
DR RefSeq; WP_000783123.1; NZ_LN832404.1.
DR AlphaFoldDB; P33359; -.
DR SMR; P33359; -.
DR ComplexPortal; CPX-4449; Low affinity betaine ABC transporter complex.
DR STRING; 511145.b2128; -.
DR TCDB; 3.A.1.12.15; the atp-binding cassette (abc) superfamily.
DR PaxDb; P33359; -.
DR PRIDE; P33359; -.
DR EnsemblBacteria; AAC75189; AAC75189; b2128.
DR EnsemblBacteria; BAE76605; BAE76605; BAE76605.
DR GeneID; 949028; -.
DR KEGG; ecj:JW2116; -.
DR KEGG; eco:b2128; -.
DR PATRIC; fig|1411691.4.peg.116; -.
DR EchoBASE; EB1947; -.
DR eggNOG; COG1174; Bacteria.
DR HOGENOM; CLU_046113_7_0_6; -.
DR InParanoid; P33359; -.
DR OMA; TAYVLQG; -.
DR PhylomeDB; P33359; -.
DR BioCyc; EcoCyc:YEHW-MON; -.
DR BioCyc; MetaCyc:YEHW-MON; -.
DR PRO; PR:P33359; -.
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:0005886; C:plasma membrane; IDA:EcoCyc.
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:0031460; P:glycine betaine transport; IDA:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..243
FT /note="Glycine betaine uptake system permease protein YehW"
FT /id="PRO_0000060255"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..46
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..206
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 50..231
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 243 AA; 25515 MW; 16D90AD1338083DA CRC64;
MKMLRDPLFW LIALFVALIF WLPYSQPLFA ALFPQLPRPV YQQESFAALA LAHFWLVGIS
SLFAVIIGTG AGIAVTRPWG AEFRPLVETI AAVGQTFPPV AVLAIAVPVI GFGLQPAIIA
LILYGVLPVL QATLAGLGAI DASVTEVAKG MGMSRGQRVR KVELPLAAPV ILAGVRTSVI
INIGTATIAS TVGASTLGTP IIIGLSGFNT AYVIQGALLV ALAAIIADRL FERLVQALSQ
HAK
