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Database: UniProt
Entry: A0A0R1W1Q7_9LACO
LinkDB: A0A0R1W1Q7_9LACO
Original site: A0A0R1W1Q7_9LACO 
ID   A0A0R1W1Q7_9LACO        Unreviewed;       261 AA.
AC   A0A0R1W1Q7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Acetyl-CoA carboxylase, carboxyl transferase subunit beta {ECO:0000313|EMBL:KRM11655.1};
GN   ORFNames=FD16_GL000572 {ECO:0000313|EMBL:KRM11655.1};
OS   Paucilactobacillus suebicus DSM 5007 = KCTC 3549.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Paucilactobacillus.
OX   NCBI_TaxID=1423807 {ECO:0000313|EMBL:KRM11655.1, ECO:0000313|Proteomes:UP000051820};
RN   [1] {ECO:0000313|EMBL:KRM11655.1, ECO:0000313|Proteomes:UP000051820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5007 {ECO:0000313|EMBL:KRM11655.1,
RC   ECO:0000313|Proteomes:UP000051820};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRM11655.1}.
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DR   EMBL; AZGF01000016; KRM11655.1; -; Genomic_DNA.
DR   RefSeq; WP_010622981.1; NZ_BACO01000068.1.
DR   AlphaFoldDB; A0A0R1W1Q7; -.
DR   STRING; 1423807.FD16_GL000572; -.
DR   PATRIC; fig|1423807.3.peg.581; -.
DR   eggNOG; COG0777; Bacteria.
DR   OrthoDB; 9772975at2; -.
DR   Proteomes; UP000051820; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011762; COA_CT_N.
DR   PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   4: Predicted;
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRM11655.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          9..261
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
SQ   SEQUENCE   261 AA;  28917 MW;  AC94EBF4E0380085 CRC64;
     MSHLPDKGVW TKCPACGGHV NQLEWGSIKK CPQCGSYQRL TIKERLTITI DDGSFEPISM
     LPNSDNLLKV AGYSEKLAEA RKKTEITEAI TVGTGSIDNK QCAIGIMDSH FMMGTLNTTV
     GDRIKQLYLF AEEKRIPLIL MIASGGARMQ EGIFSLLQMN TILAAKQQYD RCHQVSISVL
     TDPTMGGVSA SFAFKNDIVV AEDQAQIGFA GPRVIQATSQ EQLPKDFQQA SQLFAHGLID
     DRIRREDLRD YLGKLLTLHQ R
//
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