ID A0A1T1BD29_9DEIO Unreviewed; 323 AA.
AC A0A1T1BD29;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BXU09_05645 {ECO:0000313|EMBL:OOV14234.1};
OS Deinococcus sp. LM3.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1938608 {ECO:0000313|EMBL:OOV14234.1, ECO:0000313|Proteomes:UP000191141};
RN [1] {ECO:0000313|EMBL:OOV14234.1, ECO:0000313|Proteomes:UP000191141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM3 {ECO:0000313|EMBL:OOV14234.1,
RC ECO:0000313|Proteomes:UP000191141};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-2017) 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:OOV14234.1}.
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DR EMBL; MUFV01000001; OOV14234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T1BD29; -.
DR STRING; 1938608.BXU09_05645; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000191141; Unassembled WGS sequence.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
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:OOV14234.1}.
FT DOMAIN 52..247
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 323 AA; 33547 MW; D2D2B498BAC59D49 CRC64;
MPDRLLPLLT ERPQTGDALG QTLGVNRVTV NTLARHLIEA GVPVQVTRAG YALPPGTPTP
HLTPRSGTLG QAMRYQGTVT STQDSLRAWA DHPTHPAPHG AVTVAERQTA GRGRRGRTWD
TTHGTLVFSV LLTRSLRGGP LTLADLPLMP LAAGVAVQRA AGVGGLKWPN DLLAPNGRKL
AGILLEADLR GEEARRAVLG IGINVTAAPQ DAAHLGALHA PGTPEPTRAA LLGTLLLELE
RWLAAPATDI LNAWRAANVT LGRPVLIHTH EGPLEGVATD LDAQGSLIVT TAHGPRTVSA
GDVQLVGSLA PELPEPSGSG PAP
//