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   02-SEP-2026, entry version 191.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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_CP009789.1.
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   PDB; 8Q52; X-ray; 2.15 A; A=24-163, A=273-351.
DR   AlphaFoldDB; P04816; -.
DR   MDposit; P04816; -.
DR   SMR; P04816; -.
DR   BioGRID; 4262495; 39.
DR   ComplexPortal; CPX-4317; Branched chain amino acid, leucine-specific ABC transporter complex.
DR   FunCoup; P04816; 404.
DR   IntAct; P04816; 3.
DR   STRING; 511145.b3458; -.
DR   TCDB; 3.A.1.4.1; the atp-binding cassette (abc) superfamily.
DR   jPOST; P04816; -.
DR   PaxDb; 511145-b3458; -.
DR   EnsemblBacteria; AAC76483; AAC76483; b3458.
DR   GeneID; 93778533; -.
DR   GeneID; 947964; -.
DR   KEGG; ecj:JW3423; -.
DR   KEGG; eco:b3458; -.
DR   KEGG; ecoc:C3026_18730; -.
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; GFVMAKF; -.
DR   OrthoDB; 9768386at2; -.
DR   PhylomeDB; P04816; -.
DR   BioCyc; EcoCyc:LIVK-MONOMER; -.
DR   BioCyc; MetaCyc:LIVK-MONOMER; -.
DR   EvolutionaryTrace; P04816; -.
DR   PRO; PR:P04816; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P04816; -.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; NAS:ComplexPortal.
DR   GO; GO:0016020; C:membrane; NAS:ComplexPortal.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0070728; F:L-leucine binding; IPI:EcoCyc.
DR   GO; GO:0015803; P:branched-chain amino acid transport; NAS:ComplexPortal.
DR   GO; GO:0015818; P:isoleucine transport; IBA:GO_Central.
DR   GO; GO:0015820; P:L-leucine transport; IMP:EcoCyc.
DR   GO; GO:0015823; P:phenylalanine transport; NAS:ComplexPortal.
DR   GO; GO:0015829; P:valine transport; IBA:GO_Central.
DR   CDD; cd06342; PBP1_ABC_LIVBP-like; 1.
DR   FunFam; 3.40.50.2300:FF:000033; Amino acid ABC transporter substrate-binding protein; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   InterPro; IPR028081; Leu-bd.
DR   InterPro; IPR000709; Leu_Ile_Val-bd.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   NCBIfam; NF011933; PRK15404.1; 1.
DR   PANTHER; PTHR47151; LEU/ILE/VAL-BINDING ABC TRANSPORTER SUBUNIT; 1.
DR   PANTHER; PTHR47151:SF3; LEUCINE-SPECIFIC-BINDING PROTEIN; 1.
DR   Pfam; PF13458; Peripla_BP_6; 1.
DR   PRINTS; PR00337; LEUILEVALBP.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   PDBsum; 1USG; -.
DR   PDBsum; 1USI; -.
DR   PDBsum; 1USK; -.
DR   PDBsum; 2LBP; -.
DR   PDBsum; 8Q52; -.
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..154
FT                   /evidence="ECO:0007829|PDB:1USG"
FT   HELIX           155..159
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
//