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UGPE_ECOK1
ID   UGPE_ECOK1              Reviewed;         281 AA.
AC   A1AGY2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=sn-glycerol-3-phosphate transport system permease protein UgpE;
GN   Name=ugpE; OrderedLocusNames=Ecok1_34280; ORFNames=APECO1_3008;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
CC   -!- FUNCTION: Part of the binding-protein-dependent transport system for
CC       sn-glycerol-3-phosphate; probably responsible for the translocation of
CC       the substrate across the membrane. {ECO:0000250}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (UgpC),
CC       two transmembrane proteins (UgpA and UgpE) and a solute-binding protein
CC       (UgpB). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. UgpAE subfamily. {ECO:0000305}.
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DR   EMBL; CP000468; ABJ02922.1; -; Genomic_DNA.
DR   RefSeq; WP_000572183.1; NC_008563.1.
DR   AlphaFoldDB; A1AGY2; -.
DR   SMR; A1AGY2; -.
DR   EnsemblBacteria; ABJ02922; ABJ02922; APECO1_3008.
DR   GeneID; 66506595; -.
DR   KEGG; ecv:APECO1_3008; -.
DR   HOGENOM; CLU_016047_1_1_6; -.
DR   OMA; IAFFIAW; -.
DR   Proteomes; UP000008216; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IEA:InterPro.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0015794; P:glycerol-3-phosphate transmembrane transport; IEA:InterPro.
DR   GO; GO:0001407; P:glycerophosphodiester 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   InterPro; IPR030165; UgpE.
DR   PANTHER; PTHR43744:SF8; PTHR43744:SF8; 1.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..281
FT                   /note="sn-glycerol-3-phosphate transport system permease
FT                   protein UgpE"
FT                   /id="PRO_0000292676"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          77..268
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   281 AA;  31530 MW;  2CAF3F10CE4CF5A6 CRC64;
     MIENRPWLTI FSHTMLILGI AVILFPLYVA FVAATLDKQE VYAAPMTLIP GTHLLENIHN
     IWVNGVGTNS APFWRMLLNS FVMAFSITLG KITVSMLSAF AIVWFRFPLR NLFFWMIFIT
     LMLPVEVRIF PTVEVIANLK MLDSYAGLTL PLMASATATF LFRQFFMTLP DELVEAARID
     GASPMRFFCD IVFPLSKTNL AALFVITFIY GWNQYLWPLL IITDVDLGTT VAGIKGMIAT
     GEGTTEWNSV MAAMLLTLIP PVVIVLVMQR AFVRGLVDSE K
 
 
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