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Database: UniProt
Entry: P49786
LinkDB: P49786
Original site: P49786 
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   10-APR-2019, entry version 116.
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; Firmicutes; 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
RT   carboxylase, 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
RT   the Bacillus subtilis genome containing the skin element and many
RT   sporulation 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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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).
CC       Binds 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}.
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   ProteinModelPortal; P49786; -.
DR   SMR; P49786; -.
DR   STRING; 224308.BSU24350; -.
DR   jPOST; P49786; -.
DR   PaxDb; P49786; -.
DR   PRIDE; P49786; -.
DR   EnsemblBacteria; CAB14366; CAB14366; BSU24350.
DR   GeneID; 938587; -.
DR   KEGG; bsu:BSU24350; -.
DR   PATRIC; fig|224308.179.peg.2653; -.
DR   eggNOG; COG0511; LUCA.
DR   HOGENOM; HOG000008876; -.
DR   InParanoid; P49786; -.
DR   KO; K02160; -.
DR   OMA; IKSPIIG; -.
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; 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; Reference proteome.
FT   CHAIN         1    159       Biotin carboxyl carrier protein of
FT                                acetyl-CoA carboxylase.
FT                                /FTId=PRO_0000146801.
FT   DOMAIN       81    157       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   MOD_RES     123    123       N6-biotinyllysine.
FT                                {ECO:0000250|UniProtKB:P0ABD8,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   CONFLICT     64     65       AQ -> GE (in Ref. 1; AAB00182).
FT                                {ECO:0000305}.
FT   CONFLICT    126    126       N -> I (in Ref. 1; AAB00182).
FT                                {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
//
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