BCCP_STRP6
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 25-MAY-2022, entry version 77.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase;
DE Short=BCCP;
GN Name=accB {ECO:0000250|UniProtKB:P0ABD8}; 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 metagenome:
RT complete genome sequence of a macrolide-resistant serotype 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;
CC Evidence={ECO:0000269|Ref.2};
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DR EMBL; CP000003; AAT87617.1; -; Genomic_DNA.
DR RefSeq; WP_011018155.1; NC_006086.1.
DR AlphaFoldDB; Q5XAE6; -.
DR SMR; Q5XAE6; -.
DR EnsemblBacteria; AAT87617; AAT87617; M6_Spy1482.
DR KEGG; spa:M6_Spy1482; -.
DR HOGENOM; CLU_016733_3_2_9; -.
DR OMA; IKSPIIG; -.
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; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism.
FT CHAIN 1..166
FT /note="Biotin carboxyl carrier protein of acetyl-CoA
FT carboxylase"
FT /id="PRO_0000273576"
FT DOMAIN 90..166
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 61..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT 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