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Database: UniProt
Entry: R5CSW7_9FIRM
LinkDB: R5CSW7_9FIRM
Original site: R5CSW7_9FIRM 
ID   R5CSW7_9FIRM            Unreviewed;       248 AA.
AC   R5CSW7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=biotin--[biotin carboxyl-carrier protein] ligase {ECO:0000256|ARBA:ARBA00024227};
DE            EC=6.3.4.15 {ECO:0000256|ARBA:ARBA00024227};
GN   ORFNames=BN705_00150 {ECO:0000313|EMBL:CCX70933.1};
OS   Firmicutes bacterium CAG:555.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263030 {ECO:0000313|EMBL:CCX70933.1, ECO:0000313|Proteomes:UP000018402};
RN   [1] {ECO:0000313|EMBL:CCX70933.1, ECO:0000313|Proteomes:UP000018402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:555 {ECO:0000313|Proteomes:UP000018402};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCX70933.1}.
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DR   EMBL; CAWW010000020; CCX70933.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5CSW7; -.
DR   STRING; 1263030.BN705_00150; -.
DR   Proteomes; UP000018402; Unassembled WGS sequence.
DR   GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   CDD; cd16442; BPL; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR   InterPro; IPR003142; BPL_C.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   NCBIfam; TIGR00121; birA_ligase; 1.
DR   PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR   PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR   Pfam; PF02237; BPL_C; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   4: Predicted;
KW   Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCX70933.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018402}.
FT   DOMAIN          1..184
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   248 AA;  26572 MW;  83096147F1DF12F6 CRC64;
     MKKLQIKLNA FETLDSTNTY LKKLAAEGAS EGTVVIANAQ TAGRGRMGRS FASAQGLGIY
     MSLLLRPDCA ASCAQSLTAN TAAAVCMAIE TVSGVKPEIK WVNDLYLKGK KICGILCESA
     VSGDKLDYAV IGIGLNVITR PEDFPEELRH TAGSIYSQTG LIIERGKLIS AILTELDGMY
     AAWCEDKSAY LSEYKSRCTM LGRVVTVISP DGDYDALAKD ITPDFGLVVE TVDGETRTLH
     SGEISVKI
//
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