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Database: UniProt
Entry: Q5XAE6
LinkDB: Q5XAE6
Original site: Q5XAE6 
ID   BCCP_STRP6              Reviewed;         166 AA.
AC   Q5XAE6; P82580;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   28-FEB-2018, entry version 70.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase;
DE            Short=BCCP;
GN   Name=accB {ECO:0000250|UniProtKB:P0ABD8};
GN   OrderedLocusNames=M6_Spy1482;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1] {ECO:0000312|EMBL:AAT87617.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus
RT   metagenome: complete genome sequence of a macrolide-resistant serotype
RT   M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 8-19 AND 25-34, AND MASS SPECTROMETRY.
RC   STRAIN=JRS4 / Serotype M6 {ECO:0000269|Ref.2};
RA   Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA   VanBogelen R.A.;
RT   "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT   proteins.";
RL   Submitted (MAY-2000) to UniProtKB.
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:0000250|UniProtKB:P0ABD8}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0ABD8}.
CC   -!- MASS SPECTROMETRY: Mass=17883.26; Method=Electrospray; Range=1-
CC       166; Evidence={ECO:0000269|Ref.2};
DR   EMBL; CP000003; AAT87617.1; -; Genomic_DNA.
DR   RefSeq; WP_011018155.1; NC_006086.1.
DR   ProteinModelPortal; Q5XAE6; -.
DR   SMR; Q5XAE6; -.
DR   EnsemblBacteria; AAT87617; AAT87617; M6_Spy1482.
DR   KEGG; spa:M6_Spy1482; -.
DR   HOGENOM; HOG000008876; -.
DR   KO; K02160; -.
DR   OMA; IKSPIIG; -.
DR   BioCyc; SPYO286636:G1G3V-1530-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001167; Chromosome.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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   Biotin; Complete proteome; Direct protein sequencing;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism.
FT   CHAIN         1    166       Biotin carboxyl carrier protein of
FT                                acetyl-CoA carboxylase.
FT                                /FTId=PRO_0000273576.
FT   DOMAIN       90    166       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   MOD_RES     132    132       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   166 AA;  17903 MW;  626CCB1299FE29BD CRC64;
     MNIQEIKDLM AQFDTSSLRE FLFKTNEGEL IFSKNEQHLN ASISNQEHAV PVPQVQLVPN
     STASEASSPA SVKDVPVEEQ PQAESFVAEG DIVESPLVGV AYLAASPDKP PFVAVGDTVK
     KGQTLVIIEA MKVMNEVPAP CDGVITEILV SNEDVIEFGQ GLVRIK
//
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