PROX_ECOLI
ID PROX_ECOLI Reviewed; 330 AA.
AC P0AFM2; P14177;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Glycine betaine/proline betaine-binding periplasmic protein {ECO:0000305};
DE AltName: Full=GBBP {ECO:0000303|PubMed:3305496};
DE Flags: Precursor;
GN Name=proX {ECO:0000303|PubMed:2649479};
GN Synonyms=proU {ECO:0000303|PubMed:3305496};
GN OrderedLocusNames=b2679, JW2654;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2649479; DOI=10.1128/jb.171.4.1923-1931.1989;
RA Gowrishankar J.;
RT "Nucleotide sequence of the osmoregulatory proU operon of Escherichia
RT coli.";
RL J. Bacteriol. 171:1923-1931(1989).
RN [2]
RP ERRATUM OF PUBMED:2649479.
RA Gowrishankar J.;
RL J. Bacteriol. 172:1165-1165(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 22-34, FUNCTION IN GLYCINE BETAINE TRANSPORT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=3305496; DOI=10.1016/s0021-9258(18)60890-7;
RA Barron A., Jung J.U., Villarejo W.;
RT "Purification and characterization of a glycine betaine binding protein
RT from Escherichia coli.";
RL J. Biol. Chem. 262:11841-11846(1987).
RN [7]
RP FUNCTION IN PROLINE BETAINE TRANSPORT, AND SUBCELLULAR LOCATION.
RX PubMed=7898450; DOI=10.1007/bf00290728;
RA Haardt M., Kempf B., Faatz E., Bremer E.;
RT "The osmoprotectant proline betaine is a major substrate for the binding-
RT protein-dependent transport system ProU of Escherichia coli K-12.";
RL Mol. Gen. Genet. 246:783-786(1995).
RN [8]
RP INDUCTION BY COLD SHOCK.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14527658; DOI=10.1016/s0923-2508(03)00167-0;
RA Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G.,
RA Deho G.;
RT "Changes in Escherichia coli transcriptome during acclimatization at low
RT temperature.";
RL Res. Microbiol. 154:573-580(2003).
RN [9]
RP FUNCTION IN GLYCINE BETAINE TRANSPORT, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=23249124; DOI=10.3109/09687688.2012.754060;
RA Gul N., Poolman B.;
RT "Functional reconstitution and osmoregulatory properties of the ProU ABC
RT transporter from Escherichia coli.";
RL Mol. Membr. Biol. 30:138-148(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 22-330 IN COMPLEXES WITH GLYCINE
RP BETAINE AND PROLINE BETAINE, DISULFIDE BOND, AND FUNCTION.
RC STRAIN=K12;
RX PubMed=14612446; DOI=10.1074/jbc.m309771200;
RA Schiefner A., Breed J., Bosser L., Kneip S., Gade J., Holtmann G.,
RA Diederichs K., Welte W., Bremer E.;
RT "Cation-pi interactions as determinants for binding of the compatible
RT solutes glycine betaine and proline betaine by the periplasmic ligand-
RT binding protein ProX from Escherichia coli.";
RL J. Biol. Chem. 279:5588-5596(2004).
CC -!- FUNCTION: Part of the ProU ABC transporter complex involved in glycine
CC betaine and proline betaine uptake. Binds glycine betaine and proline
CC betaine with high affinity. {ECO:0000269|PubMed:14612446,
CC ECO:0000269|PubMed:23249124, ECO:0000269|PubMed:3305496,
CC ECO:0000269|PubMed:7898450}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ProV),
CC two transmembrane proteins (ProW) and a solute-binding protein (ProX).
CC {ECO:0000269|PubMed:23249124}.
CC -!- INTERACTION:
CC P0AFM2; P77165: paoA; NbExp=2; IntAct=EBI-1129961, EBI-1115563;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:3305496,
CC ECO:0000269|PubMed:7898450}.
CC -!- INDUCTION: By cold shock in a PNPase-dependent fashion.
CC {ECO:0000269|PubMed:14527658}.
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DR EMBL; M24856; AAA24429.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75726.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16544.1; -; Genomic_DNA.
DR PIR; JS0130; BLECGP.
DR RefSeq; NP_417165.1; NC_000913.3.
DR RefSeq; WP_001216525.1; NZ_LN832404.1.
DR PDB; 1R9L; X-ray; 1.59 A; A=22-330.
DR PDB; 1R9Q; X-ray; 2.05 A; A=22-330.
DR PDBsum; 1R9L; -.
DR PDBsum; 1R9Q; -.
DR AlphaFoldDB; P0AFM2; -.
DR SMR; P0AFM2; -.
DR BioGRID; 4262270; 10.
DR BioGRID; 851497; 1.
DR ComplexPortal; CPX-2126; Glycine/Proline betaine ABC transporter complex.
DR IntAct; P0AFM2; 2.
DR STRING; 511145.b2679; -.
DR DrugBank; DB04284; L-proline betaine.
DR DrugBank; DB04455; N,N,N-trimethylglycinium.
DR TCDB; 3.A.1.12.1; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P0AFM2; -.
DR jPOST; P0AFM2; -.
DR PaxDb; P0AFM2; -.
DR PRIDE; P0AFM2; -.
DR EnsemblBacteria; AAC75726; AAC75726; b2679.
DR EnsemblBacteria; BAA16544; BAA16544; BAA16544.
DR GeneID; 947165; -.
DR KEGG; ecj:JW2654; -.
DR KEGG; eco:b2679; -.
DR PATRIC; fig|1411691.4.peg.4062; -.
DR EchoBASE; EB0766; -.
DR eggNOG; COG2113; Bacteria.
DR HOGENOM; CLU_070055_0_0_6; -.
DR InParanoid; P0AFM2; -.
DR OMA; EHNQGNY; -.
DR PhylomeDB; P0AFM2; -.
DR BioCyc; EcoCyc:PROX-MON; -.
DR BioCyc; MetaCyc:PROX-MON; -.
DR EvolutionaryTrace; P0AFM2; -.
DR PRO; PR:P0AFM2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:1990222; C:ProVWX complex; IPI:ComplexPortal.
DR GO; GO:0050997; F:quaternary ammonium group binding; IPI:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0089718; P:amino acid import across plasma membrane; IDA:ComplexPortal.
DR GO; GO:0071470; P:cellular response to osmotic stress; IDA:ComplexPortal.
DR GO; GO:0031460; P:glycine betaine transport; IDA:ComplexPortal.
DR GO; GO:1903804; P:glycine import across plasma membrane; IDA:ComplexPortal.
DR GO; GO:0006972; P:hyperosmotic response; IDA:EcoCyc.
DR InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
DR Pfam; PF04069; OpuAC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Direct protein sequencing;
KW Disulfide bond; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:3305496"
FT CHAIN 22..330
FT /note="Glycine betaine/proline betaine-binding periplasmic
FT protein"
FT /id="PRO_0000031847"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:14612446"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:14612446"
FT BINDING 161..163
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:14612446"
FT DISULFID 157..163
FT /evidence="ECO:0000269|PubMed:14612446"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1R9L"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:1R9L"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1R9L"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1R9L"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1R9L"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1R9L"
FT STRAND 109..120
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1R9L"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:1R9L"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1R9L"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:1R9L"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:1R9L"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:1R9L"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:1R9L"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 283..295
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 300..313
FT /evidence="ECO:0007829|PDB:1R9L"
FT HELIX 315..326
FT /evidence="ECO:0007829|PDB:1R9L"
SQ SEQUENCE 330 AA; 36023 MW; 2B98AF52552ACD2C CRC64;
MRHSVLFATA FATLISTQTF AADLPGKGIT VNPVQSTITE ETFQTLLVSR ALEKLGYTVN
KPSEVDYNVG YTSLASGDAT FTAVNWTPLH DNMYEAAGGD KKFYREGVFV NGAAQGYLID
KKTADQYKIT NIAQLKDPKI AKLFDTNGDG KADLTGCNPG WGCEGAINHQ LAAYELTNTV
THNQGNYAAM MADTISRYKE GKPVFYYTWT PYWVSNELKP GKDVVWLQVP FSALPGDKNA
DTKLPNGANY GFPVSTMHIV ANKAWAEKNP AAAKLFAIMQ LPVADINAQN AIMHDGKASE
GDIQGHVDGW IKAHQQQFDG WVNEALAAQK
