ID   PCCB_BACSU              Reviewed;         507 AA.
AC   P54541;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Putative propionyl-CoA carboxylase beta chain;
DE            Short=PCCase;
DE            EC=6.4.1.3;
DE   AltName: Full=Propanoyl-CoA:carbon dioxide ligase;
GN   Name=yqjD; OrderedLocusNames=BSU23920;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
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   [3]
RP   SEQUENCE REVISION TO N-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-
CC         CoA + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23720,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57327, ChEBI:CHEBI:57392,
CC         ChEBI:CHEBI:456216; EC=6.4.1.3;
CC   -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC       succinyl-CoA from propanoyl-CoA: step 1/3.
CC   -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha
CC       subunits and six beta subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA12610.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D84432; BAA12610.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB14323.2; -; Genomic_DNA.
DR   PIR; D69963; D69963.
DR   RefSeq; NP_390272.2; NC_000964.3.
DR   RefSeq; WP_010886564.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P54541; -.
DR   SMR; P54541; -.
DR   STRING; 224308.BSU23920; -.
DR   PaxDb; P54541; -.
DR   PRIDE; P54541; -.
DR   EnsemblBacteria; CAB14323; CAB14323; BSU_23920.
DR   GeneID; 938685; -.
DR   KEGG; bsu:BSU23920; -.
DR   PATRIC; fig|224308.43.peg.2495; -.
DR   eggNOG; COG4799; Bacteria.
DR   InParanoid; P54541; -.
DR   OMA; YAYAECT; -.
DR   PhylomeDB; P54541; -.
DR   BioCyc; BSUB:BSU23920-MON; -.
DR   UniPathway; UPA00945; UER00908.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IBA:GO_Central.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004658; F:propionyl-CoA carboxylase activity; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..507
FT                   /note="Putative propionyl-CoA carboxylase beta chain"
FT                   /id="PRO_0000199797"
FT   DOMAIN          1..254
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          256..501
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   REGION          1..501
FT                   /note="Carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   507 AA;  55475 MW;  1D428B7B8E7BFA25 CRC64;
     MNEHMDHFYT KRKQAEEGGG REKLAQQRQK GKLTARERII FLLDQDSFIE LHPFMESQVL
     TREQRMLGDG VVTGYGTIDG RSVYVFAQDF TVYGGALGET HARKICALMD LAAKNKAPII
     GLNDSGGARI QEGVLSLDGY GHIFYRNVLY SGVIPQISVI LGPCAGGAVY SPALTDFIFM
     AEQTGRMFIT GPKVIEKVTG EQVDAESLGG AGIHNAVSGN AHFSGHTEKE VLTGVRKLLS
     YLPLNGRTTE PKPEKEASRP LLNRLVPADT TKPYDVRKVI RELADPQSFF EIQPFFAKNI
     VIGFARLGEK AIGIVASQPK HLAGSLTIDA ADKAARFIRF CDAFDIPLLT VEDVPGFLPG
     IQQEHNGIIR HGAKLLFAYA EATVPKVTLI IRKAYGGAYV AMNSKAIGAD LVFAWPNAEI
     AVMGPEGAAS ILYEKEIKAS ADPQKTKREK TAEYKKQNAG PYKAAACGMV DDIILPEESR
     GRLIQAFHML THKTEERPKK KHGNIPL