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Database: UniProt
Entry: A0A1G6CXA0_9FIRM
LinkDB: A0A1G6CXA0_9FIRM
Original site: A0A1G6CXA0_9FIRM 
ID   A0A1G6CXA0_9FIRM        Unreviewed;       256 AA.
AC   A0A1G6CXA0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=SAMN02910298_01820 {ECO:0000313|EMBL:SDB37557.1};
OS   Pseudobutyrivibrio sp. YE44.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Pseudobutyrivibrio.
OX   NCBI_TaxID=1520802 {ECO:0000313|EMBL:SDB37557.1, ECO:0000313|Proteomes:UP000198713};
RN   [1] {ECO:0000313|Proteomes:UP000198713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YE44 {ECO:0000313|Proteomes:UP000198713};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMXT01000005; SDB37557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6CXA0; -.
DR   STRING; 1520802.SAMN02910298_01820; -.
DR   OrthoDB; 9807064at2; -.
DR   Proteomes; UP000198713; 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   InterPro; IPR008988; Transcriptional_repressor_C.
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; SSF50037; C-terminal domain of transcriptional repressors; 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:SDB37557.1}.
FT   DOMAIN          1..186
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   256 AA;  28919 MW;  5DCC2B7E4AF3DB73 CRC64;
     MLNNIRYEYY ESVDSTNDRI KSRAHENENQ GLVISAGQQT AGKGRIGRKW ESPSHDSIST
     SILLKPEEIT LEAIPTITVV AAMAVRDALY RIYGLNGLIK WPNDIVLDGK KICGILTEME
     MKDGKVWFVI VGIGVNVHNK SFPEEIAFKA TSVDLELAKA GGTHGHRQEL TKEIWNSFAK
     YYNIFIETQD MSGLKEEYEK YLANRGNRVR IEDRENSYEA TALGINERGE LIVEVEGEER
     IIRTGEVSVR GIYGYI
//
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