LIVK_ECOLI
ID LIVK_ECOLI Reviewed; 369 AA.
AC P04816; Q2M7C1; Q47343;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Leucine-specific-binding protein;
DE Short=L-BP;
DE Short=LS-BP;
DE Flags: Precursor;
GN Name=livK; OrderedLocusNames=b3458, JW3423;
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=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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX PubMed=6990419; DOI=10.1073/pnas.77.4.2005;
RA Oxender D.L., Anderson J.J., Daniels C.J., Landick R., Gunsalus R.P.,
RA Zurawski G., Yanofsky C.;
RT "Amino-terminal sequence and processing of the precursor of the leucine-
RT specific binding protein, and evidence for conformational differences
RT between the precursor and the mature form.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:2005-2009(1980).
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 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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=2649683; DOI=10.1016/0022-2836(89)90532-9;
RA Sack J.S., Trakhanov S.D., Tsigannik I.H., Quiocho F.A.;
RT "Structure of the L-leucine-binding protein refined at 2.4-A resolution and
RT comparison with the Leu/Ile/Val-binding protein structure.";
RL J. Mol. Biol. 206:193-207(1989).
CC -!- FUNCTION: This protein is a component of the leucine-specific transport
CC system, which is one of the two periplasmic binding protein-dependent
CC transport systems of the high-affinity transport of the branched-chain
CC amino acids in E.coli.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the leucine-binding protein family.
CC {ECO:0000305}.
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DR EMBL; M29378; AAA24090.1; -; Genomic_DNA.
DR EMBL; J05516; AAA83883.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18433.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76483.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77835.1; -; Genomic_DNA.
DR EMBL; V00301; CAA23579.1; -; Genomic_DNA.
DR PIR; E65142; BLECL.
DR RefSeq; NP_417915.1; NC_000913.3.
DR RefSeq; WP_000827696.1; NZ_STEB01000004.1.
DR PDB; 1USG; X-ray; 1.53 A; A=24-369.
DR PDB; 1USI; X-ray; 1.80 A; A/C=24-369.
DR PDB; 1USK; X-ray; 2.00 A; A/B/C/D=24-369.
DR PDB; 2LBP; X-ray; 2.40 A; A=24-369.
DR PDBsum; 1USG; -.
DR PDBsum; 1USI; -.
DR PDBsum; 1USK; -.
DR PDBsum; 2LBP; -.
DR AlphaFoldDB; P04816; -.
DR SMR; P04816; -.
DR BioGRID; 4262495; 36.
DR ComplexPortal; CPX-4317; Branched chain amino acid, leucine-specific ABC transporter complex.
DR IntAct; P04816; 3.
DR STRING; 511145.b3458; -.
DR TCDB; 3.A.1.4.1; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P04816; -.
DR jPOST; P04816; -.
DR PaxDb; P04816; -.
DR PRIDE; P04816; -.
DR EnsemblBacteria; AAC76483; AAC76483; b3458.
DR EnsemblBacteria; BAE77835; BAE77835; BAE77835.
DR GeneID; 66672660; -.
DR GeneID; 947964; -.
DR KEGG; ecj:JW3423; -.
DR KEGG; eco:b3458; -.
DR PATRIC; fig|511145.12.peg.3556; -.
DR EchoBASE; EB0535; -.
DR eggNOG; COG0683; Bacteria.
DR HOGENOM; CLU_027128_6_0_6; -.
DR InParanoid; P04816; -.
DR OMA; YGVGFEQ; -.
DR PhylomeDB; P04816; -.
DR BioCyc; EcoCyc:LIVK-MON; -.
DR BioCyc; MetaCyc:LIVK-MON; -.
DR EvolutionaryTrace; P04816; -.
DR PRO; PR:P04816; -.
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:0070728; F:leucine binding; IPI:EcoCyc.
DR GO; GO:0015803; P:branched-chain amino acid transport; IC:ComplexPortal.
DR GO; GO:0015820; P:leucine transport; IMP:EcoCyc.
DR GO; GO:0015823; P:phenylalanine transport; IC:ComplexPortal.
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:9298646"
FT CHAIN 24..369
FT /note="Leucine-specific-binding protein"
FT /id="PRO_0000017702"
FT DISULFID 76..101
FT /evidence="ECO:0000250"
FT CONFLICT 3
FT /note="R -> A (in Ref. 7; CAA23579)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="D -> I (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="R -> E (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="N -> A (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 39..58
FT /evidence="ECO:0007829|PDB:1USG"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 298..317
FT /evidence="ECO:0007829|PDB:1USG"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:1USG"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:1USG"
SQ SEQUENCE 369 AA; 39379 MW; 42B939A18D8723B2 CRC64;
MKRNAKTIIA GMIALAISHT AMADDIKVAV VGAMSGPIAQ WGDMEFNGAR QAIKDINAKG
GIKGDKLVGV EYDDACDPKQ AVAVANKIVN DGIKYVIGHL CSSSTQPASD IYEDEGILMI
SPGATNPELT QRGYQHIMRT AGLDSSQGPT AAKYILETVK PQRIAIIHDK QQYGEGLARS
VQDGLKAANA NVVFFDGITA GEKDFSALIA RLKKENIDFV YYGGYYPEMG QMLRQARSVG
LKTQFMGPEG VGNASLSNIA GDAAEGMLVT MPKRYDQDPA NQGIVDALKA DKKDPSGPYV
WITYAAVQSL ATALERTGSD EPLALVKDLK ANGANTVIGP LNWDEKGDLK GFDFGVFQWH
ADGSSTAAK
