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 27-MAR-2024, entry version 139.
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; Pseudomonadota; 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 a
RT 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; DOI=10.1016/s0021-9258(18)48362-7;
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 subunits
RT 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., 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 1-25.
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 carboxylase,
RT which catalyzes the first committed step of lipid 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., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT 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; DOI=10.1016/s0021-9258(17)40340-1;
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 protein
RT (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., Tsuru D.,
RA 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 biotin
RT 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 coenzyme
RT A carboxylase of Escherichia coli determined by triple-resonance nuclear
RT 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 P0ABD8; P24182: accC; NbExp=10; IntAct=EBI-542320, EBI-542308;
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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_STEB01000012.1.
DR PDB; 1A6X; NMR; -; A=70-156.
DR PDB; 1BDO; X-ray; 1.80 A; A=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; 2BDO; -.
DR PDBsum; 3BDO; -.
DR PDBsum; 4HR7; -.
DR AlphaFoldDB; P0ABD8; -.
DR BMRB; P0ABD8; -.
DR SMR; P0ABD8; -.
DR BioGRID; 4259533; 408.
DR BioGRID; 852070; 1.
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 jPOST; P0ABD8; -.
DR PaxDb; 511145-b3255; -.
DR EnsemblBacteria; AAC76287; AAC76287; b3255.
DR GeneID; 75206103; -.
DR GeneID; 947758; -.
DR KEGG; ecj:JW3223; -.
DR KEGG; eco:b3255; -.
DR PATRIC; fig|1411691.4.peg.3473; -.
DR EchoBASE; EB0271; -.
DR eggNOG; COG0511; Bacteria.
DR HOGENOM; CLU_016733_3_1_6; -.
DR InParanoid; P0ABD8; -.
DR OMA; EVEYPCK; -.
DR OrthoDB; 9811735at2; -.
DR PhylomeDB; P0ABD8; -.
DR BioCyc; EcoCyc:BCCP-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; IDA:ComplexPortal.
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:0060090; F:molecular adaptor activity; EXP:DisProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:ComplexPortal.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IDA:ComplexPortal.
DR CDD; cd06850; biotinyl_domain; 1.
DR DisProt; DP00970; -.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR001249; AcCoA_biotinCC.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR00531; BCCP; 1.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR PRINTS; PR01071; ACOABIOTINCC.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biotin; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..156
FT /note="Biotin carboxyl carrier protein of acetyl-CoA
FT carboxylase"
FT /id="PRO_0000146805"
FT DOMAIN 73..156
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 122
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000269|PubMed:324999"
FT CONFLICT 113
FT /note="D -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1A6X"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1BDO"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:1BDO"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:1BDO"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1BDO"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1BDO"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3BDO"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3BDO"
FT STRAND 151..155
FT /evidence="ECO:0007829|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
//
