UGPB_ECOLI
ID UGPB_ECOLI Reviewed; 438 AA.
AC P0AG80; P10904; Q2M7B6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=sn-glycerol-3-phosphate-binding periplasmic protein UgpB;
DE Flags: Precursor;
GN Name=ugpB; OrderedLocusNames=b3453, JW3418;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3062310; DOI=10.1111/j.1365-2958.1988.tb00088.x;
RA Overduin P., Boos W., Tommassen J.;
RT "Nucleotide sequence of the ugp genes of Escherichia coli K-12: homology to
RT the maltose system.";
RL Mol. Microbiol. 2:767-775(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
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 [4]
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).
CC -!- FUNCTION: sn-glycerol-3-phosphate and glycerophosphoryl diester-binding
CC protein interacts with the binding protein-dependent transport system
CC UgpACE.
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: Periplasm.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
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DR EMBL; X13141; CAA31531.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18428.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76478.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77840.1; -; Genomic_DNA.
DR PIR; S47672; JGECGP.
DR RefSeq; NP_417910.1; NC_000913.3.
DR RefSeq; WP_000803190.1; NZ_SSZK01000008.1.
DR PDB; 4AQ4; X-ray; 1.80 A; A=24-438.
DR PDB; 6X84; X-ray; 1.25 A; A/B=24-438.
DR PDBsum; 4AQ4; -.
DR PDBsum; 6X84; -.
DR AlphaFoldDB; P0AG80; -.
DR SMR; P0AG80; -.
DR BioGRID; 4261118; 197.
DR ComplexPortal; CPX-2150; sn-glycerol-3-phosphate ABC transporter complex.
DR DIP; DIP-35942N; -.
DR IntAct; P0AG80; 16.
DR STRING; 511145.b3453; -.
DR TCDB; 3.A.1.1.3; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AG80; -.
DR PaxDb; P0AG80; -.
DR PRIDE; P0AG80; -.
DR EnsemblBacteria; AAC76478; AAC76478; b3453.
DR EnsemblBacteria; BAE77840; BAE77840; BAE77840.
DR GeneID; 947962; -.
DR KEGG; ecj:JW3418; -.
DR KEGG; eco:b3453; -.
DR PATRIC; fig|1411691.4.peg.3274; -.
DR EchoBASE; EB1040; -.
DR eggNOG; COG1653; Bacteria.
DR HOGENOM; CLU_031285_3_0_6; -.
DR InParanoid; P0AG80; -.
DR OMA; ESFSAWH; -.
DR PhylomeDB; P0AG80; -.
DR BioCyc; EcoCyc:UGPB-MON; -.
DR BioCyc; MetaCyc:UGPB-MON; -.
DR BRENDA; 7.6.2.10; 2026.
DR PRO; PR:P0AG80; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1902517; C:glycerol-3-phosphate-transporting ATPase complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0015794; P:glycerol-3-phosphate transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0001407; P:glycerophosphodiester transmembrane transport; IDA:EcoCyc.
DR InterPro; IPR006059; SBP.
DR InterPro; IPR006061; SBP_1_CS.
DR Pfam; PF13416; SBP_bac_8; 1.
DR PROSITE; PS01037; SBP_BACTERIAL_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..23
FT CHAIN 24..438
FT /note="sn-glycerol-3-phosphate-binding periplasmic protein
FT UgpB"
FT /id="PRO_0000031707"
FT CONFLICT 334
FT /note="P -> T (in Ref. 1; CAA31531)"
FT /evidence="ECO:0000305"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 35..51
FT /evidence="ECO:0007829|PDB:6X84"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:6X84"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6X84"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6X84"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:6X84"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:6X84"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:6X84"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 228..242
FT /evidence="ECO:0007829|PDB:6X84"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:6X84"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:4AQ4"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:6X84"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:6X84"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:6X84"
FT STRAND 306..315
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 318..332
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 334..344
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:6X84"
FT TURN 367..370
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 371..376
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 393..408
FT /evidence="ECO:0007829|PDB:6X84"
FT HELIX 414..435
FT /evidence="ECO:0007829|PDB:6X84"
SQ SEQUENCE 438 AA; 48449 MW; E0B9B5885B240C8D CRC64;
MKPLHYTASA LALGLALMGN AQAVTTIPFW HSMEGELGKE VDSLAQRFNA ENPDYKIVPT
YKGNYEQNLS AGIAAFRTGN APAILQVYEV GTATMMASKA IKPVYDVFKE AGIQFDESQF
VPTVSGYYSD SKTGHLLSQP FNSSTPVLYY NKDAFKKAGL DPEQPPKTWQ DLADYAAKLK
ASGMKCGYAS GWQGWIQLEN FSAWNGLPFA SKNNGFDGTD AVLEFNKPEQ VKHIAMLEEM
NKKGDFSYVG RKDESTEKFY NGDCAMTTAS SGSLANIREY AKFNYGVGMM PYDADAKDAP
QNAIIGGASL WVMQGKDKET YTGVAKFLDF LAKPENAAEW HQKTGYLPIT KAAYDLTREQ
GFYEKNPGAD TATRQMLNKP PLPFTKGLRL GNMPQIRVIV DEELESVWTG KKTPQQALDT
AVERGNQLLR RFEKSTKS
