ID   BCCP_BACSU              Reviewed;         159 AA.
AC   P49786;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-AUG-2003, sequence version 2.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000303|PubMed:7592499};
DE            Short=BCCP {ECO:0000303|PubMed:7592499};
GN   Name=accB {ECO:0000303|PubMed:7592499}; Synonyms=fabE, yqhW;
GN   OrderedLocusNames=BSU24350;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, AND
RP   BIOTIN-BINDING.
RC   STRAIN=168;
RX   PubMed=7592499; DOI=10.1128/jb.177.23.7003-7006.1995;
RA   Marini P.E., Li S.J., Gardiol D., Cronan J.E. Jr., de Mendoza D.;
RT   "The genes encoding the biotin carboxyl carrier protein and biotin
RT   carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase,
RT   the first enzyme of fatty acid synthesis.";
RL   J. Bacteriol. 177:7003-7006(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-124.
RC   STRAIN=168 / JH642;
RA   Guerout-Fleury A.M., Gonzy-Treboul G., Stragier P.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Binds
CC       biotin (PubMed:7592499). {ECO:0000250|UniProtKB:P0ABD8,
CC       ECO:0000269|PubMed:7592499}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000305|PubMed:7592499}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR   EMBL; U36245; AAB00182.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12568.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14366.1; -; Genomic_DNA.
DR   EMBL; U35252; AAA76728.1; -; Genomic_DNA.
DR   PIR; H69580; H69580.
DR   RefSeq; NP_390315.1; NC_000964.3.
DR   RefSeq; WP_003230252.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P49786; -.
DR   SMR; P49786; -.
DR   STRING; 224308.BSU24350; -.
DR   jPOST; P49786; -.
DR   PaxDb; 224308-BSU24350; -.
DR   EnsemblBacteria; CAB14366; CAB14366; BSU_24350.
DR   GeneID; 938587; -.
DR   KEGG; bsu:BSU24350; -.
DR   PATRIC; fig|224308.179.peg.2653; -.
DR   eggNOG; COG0511; Bacteria.
DR   InParanoid; P49786; -.
DR   OrthoDB; 9811735at2; -.
DR   PhylomeDB; P49786; -.
DR   BioCyc; BSUB:BSU24350-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   CDD; cd06850; biotinyl_domain; 1.
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   Biotin; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..159
FT                   /note="Biotin carboxyl carrier protein of acetyl-CoA
FT                   carboxylase"
FT                   /id="PRO_0000146801"
FT   DOMAIN          81..157
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   REGION          53..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         123
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0ABD8,
FT                   ECO:0000255|PROSITE-ProRule:PRU01066"
FT   CONFLICT        64..65
FT                   /note="AQ -> GE (in Ref. 1; AAB00182)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="N -> I (in Ref. 1; AAB00182)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   159 AA;  17229 MW;  7A185B5B3703A07F CRC64;
     MLNIKEIHEL IKAIDESTID EFVYENEGVS LKLKKHEAGT VQVMQQAPAA PVQAQAPQAV
     QPQAQQAAAP AQEAPKQDEN LHKITSPMVG TFYASSSPEA GPYVTAGSKV NENTVVCIVE
     AMKLFNEIEA EVKGEIVEVL VENGQLVEYG QPLFLVKAE
//