LIVJ_ECOLI
ID LIVJ_ECOLI Reviewed; 367 AA.
AC P0AD96; P02917; P76698; Q2M7C3; Q8CVL7; Q8X6S2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Leu/Ile/Val-binding protein;
DE Short=LIV-BP;
DE Flags: Precursor;
GN Name=livJ; OrderedLocusNames=b3460, JW3425;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=3891753; DOI=10.1016/s0021-9258(17)39464-4;
RA Landick R., Oxender D.L.;
RT "The complete nucleotide sequences of the Escherichia coli LIV-BP and LS-BP
RT genes. Implications for the mechanism of high-affinity branched-chain amino
RT acid transport.";
RL J. Biol. Chem. 260:8257-8261(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=4077929; DOI=10.1002/jcb.240290305;
RA Antonucci T.K., Landick R., Oxender D.L.;
RT "The leucine binding proteins of Escherichia coli as models for studying
RT the relationships between protein structure and function.";
RL J. Cell. Biochem. 29:209-216(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2195019; DOI=10.1016/s0021-9258(19)38417-0;
RA Adams M.D., Wagner L.M., Graddis T.J., Landick R., Antonucci T.K.,
RA Gibson A.L., Oxender D.L.;
RT "Nucleotide sequence and genetic characterization reveal six essential
RT genes for the LIV-I and LS transport systems of Escherichia coli.";
RL J. Biol. Chem. 265:11436-11443(1990).
RN [4]
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 [5]
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 24-367.
RC STRAIN=K12;
RX PubMed=328304; DOI=10.1016/0014-5793(77)80331-1;
RA Ovchinnikov Y.A., Aldanova N.A., Grinkevich V.A., Arzamazova N.M.,
RA Moroz I.N.;
RT "The primary structure of a Leu, Ile and Val (LIV)-binding protein from
RT Escherichia coli.";
RL FEBS Lett. 78:313-316(1977).
RN [8]
RP PROTEIN SEQUENCE OF 24-35.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP PROTEIN SEQUENCE OF 24-35.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [10]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=2649682; DOI=10.1016/0022-2836(89)90531-7;
RA Sack J.S., Saper M.A., Quiocho F.A.;
RT "Periplasmic binding protein structure and function. Refined X-ray
RT structures of the leucine/isoleucine/valine-binding protein and its complex
RT with leucine.";
RL J. Mol. Biol. 206:171-191(1989).
CC -!- FUNCTION: This protein is a component of the leucine, isoleucine,
CC valine, (threonine) transport system, which is one of the two
CC periplasmic binding protein-dependent transport systems of the high-
CC affinity transport of the branched-chain amino acids.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the leucine-binding protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18435.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J05516; AAA83881.1; -; Genomic_DNA.
DR EMBL; M29377; AAA24075.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18435.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAT48185.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77833.1; -; Genomic_DNA.
DR PIR; G65142; BLEC.
DR RefSeq; WP_001021996.1; NZ_SSZK01000008.1.
DR RefSeq; YP_026223.1; NC_000913.3.
DR PDB; 1Z15; X-ray; 1.70 A; A=24-367.
DR PDB; 1Z16; X-ray; 1.72 A; A=24-367.
DR PDB; 1Z17; X-ray; 1.96 A; A=24-367.
DR PDB; 1Z18; X-ray; 2.10 A; A=24-367.
DR PDB; 2LIV; X-ray; 2.40 A; A=24-367.
DR PDBsum; 1Z15; -.
DR PDBsum; 1Z16; -.
DR PDBsum; 1Z17; -.
DR PDBsum; 1Z18; -.
DR PDBsum; 2LIV; -.
DR AlphaFoldDB; P0AD96; -.
DR SMR; P0AD96; -.
DR BioGRID; 4259328; 24.
DR ComplexPortal; CPX-4316; Branched chain amino acid ABC transporter complex.
DR IntAct; P0AD96; 4.
DR STRING; 511145.b3460; -.
DR TCDB; 3.A.1.4.1; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P0AD96; -.
DR jPOST; P0AD96; -.
DR PaxDb; P0AD96; -.
DR PRIDE; P0AD96; -.
DR EnsemblBacteria; AAT48185; AAT48185; b3460.
DR EnsemblBacteria; BAE77833; BAE77833; BAE77833.
DR GeneID; 66672656; -.
DR GeneID; 947971; -.
DR KEGG; ecj:JW3425; -.
DR KEGG; eco:b3460; -.
DR PATRIC; fig|511145.12.peg.3559; -.
DR EchoBASE; EB0534; -.
DR eggNOG; COG0683; Bacteria.
DR HOGENOM; CLU_027128_6_0_6; -.
DR InParanoid; P0AD96; -.
DR OMA; MEFTGAR; -.
DR PhylomeDB; P0AD96; -.
DR BioCyc; EcoCyc:LIVJ-MON; -.
DR BioCyc; MetaCyc:LIVJ-MON; -.
DR EvolutionaryTrace; P0AD96; -.
DR PRO; PR:P0AD96; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0015803; P:branched-chain amino acid transport; IC:ComplexPortal.
DR GO; GO:0015818; P:isoleucine transport; IMP:EcoCyc.
DR GO; GO:0015820; P:leucine transport; IMP:EcoCyc.
DR GO; GO:0015829; P:valine transport; IMP:EcoCyc.
DR InterPro; IPR028081; Leu-bd.
DR InterPro; IPR000709; Leu_Ile_Val-bd.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF13458; Peripla_BP_6; 1.
DR PRINTS; PR00337; LEUILEVALBP.
DR SUPFAM; SSF53822; SSF53822; 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..23
FT /evidence="ECO:0000269|PubMed:328304,
FT ECO:0000269|PubMed:9298646, ECO:0000269|Ref.9"
FT CHAIN 24..367
FT /note="Leu/Ile/Val-binding protein"
FT /id="PRO_0000017700"
FT DISULFID 76..101
FT CONFLICT 3
FT /note="I -> T (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="C -> L (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="A -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="V -> A (in Ref. 1, 2, 3 and 7)"
FT /evidence="ECO:0000305"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 39..58
FT /evidence="ECO:0007829|PDB:1Z15"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 298..314
FT /evidence="ECO:0007829|PDB:1Z15"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1Z15"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:1Z15"
SQ SEQUENCE 367 AA; 39076 MW; 63F0729C251F18FD CRC64;
MNIKGKALLA GCIALAFSNM ALAEDIKVAV VGAMSGPVAQ YGDQEFTGAE QAVADINAKG
GIKGNKLQIV KYDDACDPKQ AVAVANKVVN DGIKYVIGHL CSSSTQPASD IYEDEGILMI
TPAATAPELT ARGYQLILRT TGLDSDQGPT AAKYILEKVK PQRIAIVHDK QQYGEGLARA
VQDGLKKGNA NVVFFDGITA GEKDFSTLVA RLKKENIDFV YYGGYHPEMG QILRQARAAG
LKTQFMGPEG VANVSLSNIA GESAEGLLVT KPKNYDQVPA NKPIVDAIKA KKQDPSGAFV
WTTYAALQSL QAGLNQSDDP AEIAKYLKAN SVDTVMGPLT WDEKGDLKGF EFGVFDWHAN
GTATDAK
