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Database: UniProt
Entry: P0ABD8
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ID   BCCP_ECOLI              Reviewed;         156 AA.
AC   P0ABD8; P02905; Q2M8W0;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   10-APR-2019, entry version 112.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000303|PubMed:4934522};
DE            Short=BCCP {ECO:0000303|PubMed:4934522};
GN   Name=accB; Synonyms=fabE; OrderedLocusNames=b3255, JW3223;
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;
RX   PubMed=2660106; DOI=10.1093/nar/17.10.3982;
RA   Muramatsu S., Mizuno T.;
RT   "Nucleotide sequence of the fabE gene and flanking regions containing
RT   a bent DNA sequence of Escherichia coli.";
RL   Nucleic Acids Res. 17:3982-3982(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2575489; DOI=10.1089/dna.1989.8.779;
RA   Alix J.-H.;
RT   "A rapid procedure for cloning genes from lambda libraries by
RT   complementation of E. coli defective mutants: application to the fabE
RT   region of the E. coli chromosome.";
RL   DNA 8:779-789(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1370469;
RA   Li S.-J., Cronan J.E. Jr.;
RT   "The gene encoding the biotin carboxylase subunit of Escherichia coli
RT   acetyl-CoA carboxylase.";
RL   J. Biol. Chem. 267:855-863(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Best E.A., Knauf V.C.;
RT   "Cloning and characterization of the E. coli fabEG operon encoding
RT   subunits of acetyl-CoA carboxylase.";
RL   Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Mau B., 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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX   PubMed=7678242; DOI=10.1128/jb.175.2.332-340.1993;
RA   Li S.-J., Cronan J.E. Jr.;
RT   "Growth rate regulation of Escherichia coli acetyl coenzyme A
RT   carboxylase, which catalyzes the first committed step of lipid
RT   biosynthesis.";
RL   J. Bacteriol. 175:332-340(1993).
RN   [8]
RP   PROTEIN SEQUENCE OF 1-4.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA   Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M.,
RA   Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D.,
RA   Williams K.L., Hochstrasser D.F.;
RT   "Protein identification with N and C-terminal sequence tags in
RT   proteome projects.";
RL   J. Mol. Biol. 278:599-608(1998).
RN   [9]
RP   PROTEIN SEQUENCE OF 75-156, AND BIOTINYLATION AT LYS-122.
RX   PubMed=324999;
RA   Sutton M.R., Fall R.R., Nervi A.M., Alberts A.W., Vagelos P.R.,
RA   Bradshaw R.A.;
RT   "Amino acid sequence of Escherichia coli biotin carboxyl carrier
RT   protein (9100).";
RL   J. Biol. Chem. 252:3934-3940(1977).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-156.
RC   STRAIN=K12;
RX   PubMed=1682920; DOI=10.1073/pnas.88.21.9730;
RA   Kondo H., Shiratsuchi K., Yoshimoto T., Masuda T., Kitazono A.,
RA   Tsuru D., Anai M., Sekiguchi M., Tanabe T.;
RT   "Acetyl-CoA carboxylase from Escherichia coli: gene organization and
RT   nucleotide sequence of the biotin carboxylase subunit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:9730-9733(1991).
RN   [11]
RP   FUNCTION, AND BIOTIN-BINDING.
RX   PubMed=4934522; DOI=10.1073/pnas.68.7.1512;
RA   Fall R.R., Nervi A.M., Alberts A.W., Vagelos P.R.;
RT   "Acetyl CoA carboxylase: isolation and characterization of native
RT   biotin carboxyl carrier protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 68:1512-1515(1971).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 77-156.
RX   PubMed=8747466; DOI=10.1016/S0969-2126(01)00277-5;
RA   Athappilly F.K., Hendrickson W.A.;
RT   "Structure of the biotinyl domain of acetyl-coenzyme A carboxylase
RT   determined by MAD phasing.";
RL   Structure 3:1407-1419(1995).
RN   [13]
RP   STRUCTURE BY NMR OF 70-156.
RX   PubMed=9398236; DOI=10.1021/bi971485f;
RA   Yao X., Wei D., Soden C. Jr., Summers M.F., Beckett D.;
RT   "Structure of the carboxy-terminal fragment of the apo-biotin carboxyl
RT   carrier subunit of Escherichia coli acetyl-CoA carboxylase.";
RL   Biochemistry 36:15089-15100(1997).
RN   [14]
RP   STRUCTURE BY NMR OF 77-156.
RX   PubMed=10213607; DOI=10.1021/bi982466o;
RA   Roberts E.L., Shu N., Howard M.J., Broadhurst R.W., Chapman-Smith A.,
RA   Wallace J.C., Morris T., Cronan J.E. Jr., Perham R.N.;
RT   "Solution structures of apo and holo biotinyl domains from acetyl
RT   coenzyme A carboxylase of Escherichia coli determined by triple-
RT   resonance nuclear magnetic resonance spectroscopy.";
RL   Biochemistry 38:5045-5053(1999).
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA.
CC       {ECO:0000269|PubMed:4934522}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       P24182:accC; NbExp=10; IntAct=EBI-542320, EBI-542308;
DR   EMBL; X14825; CAA32933.1; -; Genomic_DNA.
DR   EMBL; M80458; AAA23408.1; -; Genomic_DNA.
DR   EMBL; M32214; AAA23744.1; -; Genomic_DNA.
DR   EMBL; M83198; AAA23745.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA58058.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76287.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77296.1; -; Genomic_DNA.
DR   EMBL; S52932; AAB24892.1; -; mRNA.
DR   EMBL; M79446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A93687; BKEC9.
DR   RefSeq; NP_417721.1; NC_000913.3.
DR   RefSeq; WP_000354622.1; NZ_LN832404.1.
DR   PDB; 1A6X; NMR; -; A=70-156.
DR   PDB; 1BDO; X-ray; 1.80 A; A=77-156.
DR   PDB; 1K67; Model; -; B=77-155.
DR   PDB; 1K69; Model; -; B=77-156.
DR   PDB; 2BDO; NMR; -; A=77-156.
DR   PDB; 3BDO; NMR; -; A=75-156.
DR   PDB; 4HR7; X-ray; 2.50 A; B/D/G/I=1-156.
DR   PDBsum; 1A6X; -.
DR   PDBsum; 1BDO; -.
DR   PDBsum; 1K67; -.
DR   PDBsum; 1K69; -.
DR   PDBsum; 2BDO; -.
DR   PDBsum; 3BDO; -.
DR   PDBsum; 4HR7; -.
DR   DisProt; DP00970; -.
DR   ProteinModelPortal; P0ABD8; -.
DR   SMR; P0ABD8; -.
DR   BioGrid; 4259533; 408.
DR   ComplexPortal; CPX-3206; Acetyl-CoA carboxylase complex.
DR   DIP; DIP-48007N; -.
DR   IntAct; P0ABD8; 12.
DR   STRING; 511145.b3255; -.
DR   SWISS-2DPAGE; P0ABD8; -.
DR   EPD; P0ABD8; -.
DR   jPOST; P0ABD8; -.
DR   PaxDb; P0ABD8; -.
DR   PRIDE; P0ABD8; -.
DR   EnsemblBacteria; AAC76287; AAC76287; b3255.
DR   EnsemblBacteria; BAE77296; BAE77296; BAE77296.
DR   GeneID; 947758; -.
DR   KEGG; ecj:JW3223; -.
DR   KEGG; eco:b3255; -.
DR   PATRIC; fig|1411691.4.peg.3473; -.
DR   EchoBASE; EB0271; -.
DR   EcoGene; EG10275; accB.
DR   eggNOG; ENOG4105KM4; Bacteria.
DR   eggNOG; COG0511; LUCA.
DR   HOGENOM; HOG000008875; -.
DR   InParanoid; P0ABD8; -.
DR   KO; K02160; -.
DR   PhylomeDB; P0ABD8; -.
DR   BioCyc; EcoCyc:BCCP-MONOMER; -.
DR   BioCyc; ECOL316407:JW3223-MONOMER; -.
DR   BioCyc; MetaCyc:BCCP-MONOMER; -.
DR   BRENDA; 6.4.1.2; 2026.
DR   SABIO-RK; P0ABD8; -.
DR   UniPathway; UPA00094; -.
DR   EvolutionaryTrace; P0ABD8; -.
DR   PRO; PR:P0ABD8; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IC:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IMP:EcoliWiki.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0009305; P:protein biotinylation; IMP:CAFA.
DR   InterPro; IPR001249; AcCoA_biotinCC.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   PRINTS; PR01071; ACOABIOTINCC.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR00531; BCCP; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Biotin; Complete proteome; Direct protein sequencing;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome.
FT   CHAIN         1    156       Biotin carboxyl carrier protein of
FT                                acetyl-CoA carboxylase.
FT                                /FTId=PRO_0000146805.
FT   DOMAIN       73    156       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   MOD_RES     122    122       N6-biotinyllysine. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066,
FT                                ECO:0000269|PubMed:324999}.
FT   CONFLICT    113    113       D -> N (in Ref. 2). {ECO:0000305}.
FT   STRAND       72     76       {ECO:0000244|PDB:1A6X}.
FT   STRAND       80     84       {ECO:0000244|PDB:1BDO}.
FT   STRAND       86     96       {ECO:0000244|PDB:1BDO}.
FT   STRAND      114    120       {ECO:0000244|PDB:1BDO}.
FT   STRAND      123    128       {ECO:0000244|PDB:1BDO}.
FT   STRAND      133    138       {ECO:0000244|PDB:1BDO}.
FT   STRAND      142    145       {ECO:0000244|PDB:3BDO}.
FT   STRAND      148    150       {ECO:0000244|PDB:3BDO}.
FT   STRAND      151    155       {ECO:0000244|PDB:1BDO}.
SQ   SEQUENCE   156 AA;  16687 MW;  05FFDCB912A683A3 CRC64;
     MDIRKIKKLI ELVEESGISE LEISEGEESV RISRAAPAAS FPVMQQAYAA PMMQQPAQSN
     AAAPATVPSM EAPAAAEISG HIVRSPMVGT FYRTPSPDAK AFIEVGQKVN VGDTLCIVEA
     MKMMNQIEAD KSGTVKAILV ESGQPVEFDE PLVVIE
//
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