YEHY_ECOLI
ID YEHY_ECOLI Reviewed; 385 AA.
AC P33361; P76435; Q2MAU9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Glycine betaine uptake system permease protein YehY {ECO:0000305};
GN Name=yehY; OrderedLocusNames=b2130, JW2118;
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 -!- INTERACTION:
CC P33361; P0ABE2: bolA; NbExp=3; IntAct=EBI-545876, EBI-545774;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60493.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U00007; AAA60493.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75191.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76607.1; -; Genomic_DNA.
DR PIR; A64981; A64981.
DR RefSeq; NP_416634.1; NC_000913.3.
DR RefSeq; WP_000220837.1; NZ_LN832404.1.
DR AlphaFoldDB; P33361; -.
DR SMR; P33361; -.
DR BioGRID; 4260449; 12.
DR BioGRID; 851002; 3.
DR ComplexPortal; CPX-4449; Low affinity betaine ABC transporter complex.
DR DIP; DIP-11913N; -.
DR IntAct; P33361; 2.
DR STRING; 511145.b2130; -.
DR TCDB; 3.A.1.12.15; the atp-binding cassette (abc) superfamily.
DR PaxDb; P33361; -.
DR PRIDE; P33361; -.
DR EnsemblBacteria; AAC75191; AAC75191; b2130.
DR EnsemblBacteria; BAE76607; BAE76607; BAE76607.
DR GeneID; 946660; -.
DR KEGG; ecj:JW2118; -.
DR KEGG; eco:b2130; -.
DR PATRIC; fig|1411691.4.peg.114; -.
DR EchoBASE; EB1949; -.
DR eggNOG; COG1174; Bacteria.
DR HOGENOM; CLU_046113_3_0_6; -.
DR InParanoid; P33361; -.
DR OMA; GMAQFAP; -.
DR PhylomeDB; P33361; -.
DR BioCyc; EcoCyc:YEHY-MON; -.
DR BioCyc; MetaCyc:YEHY-MON; -.
DR PRO; PR:P33361; -.
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..385
FT /note="Glycine betaine uptake system permease protein YehY"
FT /id="PRO_0000060256"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..44
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..106
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..180
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..247
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..345
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 177..372
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT CONFLICT 346..385
FT /note="LLSSAIDLVLLGVIPVIVLAVLTDALFDLLIALLKVKRND -> AAKQRH
FT (in Ref. 1; AAA60493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 41139 MW; E57055E3A2B141CC CRC64;
MTYFRINPVL ALLLLLTAIA AALPFISYAP NRLVSGEGRH LWQLWPQTIW MLVGVGCAWL
TACFIPGKKG SICALILAQF VFVLLVWGAG KAATQLAQNG SALARTSLGS GFWLAAALAL
LACSDAIRRI STHPLWRWLL HMQIAIIPLW LLYSGTLNDL SLMKEYANRQ DVFDDALAQH
LTLLFGAVLP ALVIGVPLGI WCYFSTARQG AIFSLLNVIQ TVPSVALFGL LIAPLAALVT
AFPWLGTLGI AGTGMTPALI ALVLYALLPL VRGVVVGLNQ IPRDVLESAR AMGMSGAQRF
LHVQLPLALP VFLRSLRVVM VQTVGMAVIA ALIGAGGFGA LVFQGLLSSA IDLVLLGVIP
VIVLAVLTDA LFDLLIALLK VKRND