UGPA_ECO57
ID UGPA_ECO57 Reviewed; 295 AA.
AC Q7AA80; Q8X6U2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=sn-glycerol-3-phosphate transport system permease protein UgpA;
GN Name=ugpA; OrderedLocusNames=Z4820, ECs4298;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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:0000250}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. UgpAE subfamily. {ECO:0000305}.
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DR EMBL; AE005174; AAG58558.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37721.1; -; Genomic_DNA.
DR PIR; B86012; B86012.
DR PIR; B91166; B91166.
DR RefSeq; NP_312325.1; NC_002695.1.
DR RefSeq; WP_000099297.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q7AA80; -.
DR SMR; Q7AA80; -.
DR STRING; 155864.EDL933_4659; -.
DR EnsemblBacteria; AAG58558; AAG58558; Z4820.
DR EnsemblBacteria; BAB37721; BAB37721; ECs_4298.
DR GeneID; 915848; -.
DR KEGG; ece:Z4820; -.
DR KEGG; ecs:ECs_4298; -.
DR PATRIC; fig|386585.9.peg.4489; -.
DR eggNOG; COG1175; Bacteria.
DR HOGENOM; CLU_016047_0_2_6; -.
DR OMA; LWYSVQS; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..295
FT /note="sn-glycerol-3-phosphate transport system permease
FT protein UgpA"
FT /id="PRO_0000292821"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 33..80
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 102..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 131..156
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 178..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 229..262
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 284..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 76..284
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 295 AA; 33294 MW; 22FE878AFE62893F CRC64;
MSSSRPVFRS RWLPYLLVAP QLIITVIFFI WPAGEALWYS LQSVDPFGFS SRFVGLDNFV
ALFHDSYYID SFWTTIKFST FVTVSGLLVS LFFAALVEYI VRGSRFYQTL MLLPYAVAPA
VAAVLWIFLF NPGRGLITHF LAEFGYDWNH AQNSGQAMFL VVFASVWKQI SYNFLFFYAA
LQSIPRSLIE AAAIDGAGPI RRFFKIALPL IAPVSFFLLV VNLVYAFFDT FPVIDAATSG
GPVQATTTLI YKIYREGFTG LDLASSAAQS VVLMFLVIVL TVMQFRYVES KVRYQ
