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Glycine betaine/proline betaine-binding periplasmic protein (GBBP)

 PROX_ECOLI              Reviewed;         330 AA.
P0AFM2; P14177;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
20-JUN-2018, entry version 92.
RecName: Full=Glycine betaine/proline betaine-binding periplasmic protein {ECO:0000305};
AltName: Full=GBBP {ECO:0000303|PubMed:3305496};
Flags: Precursor;
Name=proX {ECO:0000303|PubMed:2649479};
Synonyms=proU {ECO:0000303|PubMed:3305496};
OrderedLocusNames=b2679, JW2654;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2649479; DOI=10.1128/jb.171.4.1923-1931.1989;
Gowrishankar J.;
"Nucleotide sequence of the osmoregulatory proU operon of Escherichia
coli.";
J. Bacteriol. 171:1923-1931(1989).
[2]
ERRATUM.
Gowrishankar J.;
J. Bacteriol. 172:1165-1165(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-
K12 genome corresponding to 50.0-68.8 min on the linkage map and
analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 22-34, FUNCTION IN GLYCINE BETAINE TRANSPORT, AND
SUBCELLULAR LOCATION.
PubMed=3305496;
Barron A., Jung J.U., Villarejo W.;
"Purification and characterization of a glycine betaine binding
protein from Escherichia coli.";
J. Biol. Chem. 262:11841-11846(1987).
[7]
FUNCTION IN PROLINE BETAINE TRANSPORT, AND SUBCELLULAR LOCATION.
PubMed=7898450; DOI=10.1007/BF00290728;
Haardt M., Kempf B., Faatz E., Bremer E.;
"The osmoprotectant proline betaine is a major substrate for the
binding-protein-dependent transport system ProU of Escherichia coli K-
12.";
Mol. Gen. Genet. 246:783-786(1995).
[8]
INDUCTION BY COLD SHOCK.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=14527658; DOI=10.1016/S0923-2508(03)00167-0;
Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V.,
Pesole G., Deho G.;
"Changes in Escherichia coli transcriptome during acclimatization at
low temperature.";
Res. Microbiol. 154:573-580(2003).
[9]
FUNCTION IN GLYCINE BETAINE TRANSPORT, AND SUBUNIT.
STRAIN=K12;
PubMed=23249124; DOI=10.3109/09687688.2012.754060;
Gul N., Poolman B.;
"Functional reconstitution and osmoregulatory properties of the ProU
ABC transporter from Escherichia coli.";
Mol. Membr. Biol. 30:138-148(2013).
[10]
X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 22-330 IN COMPLEXES WITH
GLYCINE BETAINE AND PROLINE BETAINE, DISULFIDE BOND, AND FUNCTION.
STRAIN=K12;
PubMed=14612446; DOI=10.1074/jbc.M309771200;
Schiefner A., Breed J., Bosser L., Kneip S., Gade J., Holtmann G.,
Diederichs K., Welte W., Bremer E.;
"Cation-pi interactions as determinants for binding of the compatible
solutes glycine betaine and proline betaine by the periplasmic ligand-
binding protein ProX from Escherichia coli.";
J. Biol. Chem. 279:5588-5596(2004).
-!- FUNCTION: Part of the ProU ABC transporter complex involved in
glycine betaine and proline betaine uptake. Binds glycine betaine
and proline betaine with high affinity.
{ECO:0000269|PubMed:14612446, ECO:0000269|PubMed:23249124,
ECO:0000269|PubMed:3305496, ECO:0000269|PubMed:7898450}.
-!- SUBUNIT: The complex is composed of two ATP-binding proteins
(ProV), two transmembrane proteins (ProW) and a solute-binding
protein (ProX). {ECO:0000269|PubMed:23249124}.
-!- INTERACTION:
P77165:yagT; NbExp=2; IntAct=EBI-1129961, EBI-1115563;
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:3305496,
ECO:0000269|PubMed:7898450}.
-!- INDUCTION: By cold shock in a PNPase-dependent fashion.
{ECO:0000269|PubMed:14527658}.
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EMBL; M24856; AAA24429.1; -; Genomic_DNA.
EMBL; U00096; AAC75726.1; -; Genomic_DNA.
EMBL; AP009048; BAA16544.1; -; Genomic_DNA.
PIR; JS0130; BLECGP.
RefSeq; NP_417165.1; NC_000913.3.
RefSeq; WP_001216525.1; NZ_LN832404.1.
PDB; 1R9L; X-ray; 1.59 A; A=22-330.
PDB; 1R9Q; X-ray; 2.05 A; A=22-330.
PDBsum; 1R9L; -.
PDBsum; 1R9Q; -.
ProteinModelPortal; P0AFM2; -.
SMR; P0AFM2; -.
BioGrid; 4262270; 10.
ComplexPortal; CPX-2126; ProVWX complex.
IntAct; P0AFM2; 2.
STRING; 316385.ECDH10B_2845; -.
DrugBank; DB04284; Proline Betaine.
DrugBank; DB04455; Trimethyl Glycine.
TCDB; 3.A.1.12.1; the atp-binding cassette (abc) superfamily.
SWISS-2DPAGE; P0AFM2; -.
PaxDb; P0AFM2; -.
PRIDE; P0AFM2; -.
EnsemblBacteria; AAC75726; AAC75726; b2679.
EnsemblBacteria; BAA16544; BAA16544; BAA16544.
GeneID; 947165; -.
KEGG; ecj:JW2654; -.
KEGG; eco:b2679; -.
PATRIC; fig|1411691.4.peg.4062; -.
EchoBASE; EB0766; -.
EcoGene; EG10773; proX.
eggNOG; ENOG4105GIJ; Bacteria.
eggNOG; COG2113; LUCA.
HOGENOM; HOG000282038; -.
InParanoid; P0AFM2; -.
KO; K02002; -.
OMA; EHNQGNY; -.
PhylomeDB; P0AFM2; -.
BioCyc; EcoCyc:PROX-MONOMER; -.
BioCyc; MetaCyc:PROX-MONOMER; -.
EvolutionaryTrace; P0AFM2; -.
PRO; PR:P0AFM2; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0050997; F:quaternary ammonium group binding; IPI:EcoCyc.
GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
GO; GO:0031460; P:glycine betaine transport; IDA:EcoCyc.
GO; GO:0006972; P:hyperosmotic response; IDA:EcoCyc.
InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
Pfam; PF04069; OpuAC; 1.
1: Evidence at protein level;
3D-structure; Amino-acid transport; Complete proteome;
Direct protein sequencing; Disulfide bond; Periplasm;
Reference proteome; Signal; Transport.
SIGNAL 1 21 {ECO:0000269|PubMed:3305496}.
CHAIN 22 330 Glycine betaine/proline betaine-binding
periplasmic protein.
/FTId=PRO_0000031847.
REGION 161 163 Substrate binding.
{ECO:0000269|PubMed:14612446}.
BINDING 86 86 Substrate. {ECO:0000269|PubMed:14612446}.
BINDING 90 90 Substrate. {ECO:0000269|PubMed:14612446}.
DISULFID 157 163 {ECO:0000269|PubMed:14612446}.
TURN 25 28 {ECO:0000244|PDB:1R9L}.
STRAND 33 35 {ECO:0000244|PDB:1R9L}.
HELIX 39 41 {ECO:0000244|PDB:1R9L}.
HELIX 42 54 {ECO:0000244|PDB:1R9L}.
HELIX 67 76 {ECO:0000244|PDB:1R9L}.
STRAND 77 79 {ECO:0000244|PDB:1R9L}.
STRAND 81 87 {ECO:0000244|PDB:1R9L}.
TURN 88 90 {ECO:0000244|PDB:1R9L}.
HELIX 91 96 {ECO:0000244|PDB:1R9L}.
HELIX 99 101 {ECO:0000244|PDB:1R9L}.
STRAND 103 105 {ECO:0000244|PDB:1R9L}.
STRAND 109 120 {ECO:0000244|PDB:1R9L}.
HELIX 121 127 {ECO:0000244|PDB:1R9L}.
HELIX 132 136 {ECO:0000244|PDB:1R9L}.
HELIX 138 141 {ECO:0000244|PDB:1R9L}.
HELIX 142 144 {ECO:0000244|PDB:1R9L}.
STRAND 146 155 {ECO:0000244|PDB:1R9L}.
HELIX 162 173 {ECO:0000244|PDB:1R9L}.
TURN 177 179 {ECO:0000244|PDB:1R9L}.
STRAND 180 183 {ECO:0000244|PDB:1R9L}.
HELIX 187 199 {ECO:0000244|PDB:1R9L}.
STRAND 205 213 {ECO:0000244|PDB:1R9L}.
HELIX 214 217 {ECO:0000244|PDB:1R9L}.
TURN 220 222 {ECO:0000244|PDB:1R9L}.
STRAND 223 226 {ECO:0000244|PDB:1R9L}.
STRAND 254 262 {ECO:0000244|PDB:1R9L}.
HELIX 263 268 {ECO:0000244|PDB:1R9L}.
HELIX 270 278 {ECO:0000244|PDB:1R9L}.
HELIX 283 295 {ECO:0000244|PDB:1R9L}.
HELIX 300 313 {ECO:0000244|PDB:1R9L}.
HELIX 315 326 {ECO:0000244|PDB:1R9L}.
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


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