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Database: UniProt
Entry: A0A159Z2Y7_9RHOB
LinkDB: A0A159Z2Y7_9RHOB
Original site: A0A159Z2Y7_9RHOB 
ID   A0A159Z2Y7_9RHOB        Unreviewed;       261 AA.
AC   A0A159Z2Y7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=AKL17_2221 {ECO:0000313|EMBL:AMY69467.1};
OS   Frigidibacter mobilis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Frigidibacter.
OX   NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY69467.1, ECO:0000313|Proteomes:UP000076128};
RN   [1] {ECO:0000313|EMBL:AMY69467.1, ECO:0000313|Proteomes:UP000076128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA   Geng S., Pan X., Wu X.;
RT   "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT   oilfield in Xinjiang.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) +
CC         N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-
CC         COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215;
CC         EC=6.3.4.15; Evidence={ECO:0000256|ARBA:ARBA00000933};
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DR   EMBL; CP012661; AMY69467.1; -; Genomic_DNA.
DR   RefSeq; WP_066813189.1; NZ_CP012661.1.
DR   AlphaFoldDB; A0A159Z2Y7; -.
DR   STRING; 1335048.AKL17_2221; -.
DR   KEGG; daa:AKL17_2221; -.
DR   PATRIC; fig|1335048.3.peg.2316; -.
DR   OrthoDB; 9807064at2; -.
DR   Proteomes; UP000076128; Chromosome.
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   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:AMY69467.1}.
FT   DOMAIN          6..199
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   261 AA;  27156 MW;  CE19AA441A34F869 CRC64;
     MSGSTDSRAT EPWAWPEGVA RHVLPEVDST NAEAARLAPY LTQPTWILAL RQTAARARRG
     RSWQNTPGNF AATLLMRPGG SPQEAALRSF VAALAVHEAL GSLAGPSASL ALKWPNDVLL
     NGGKVSGILL ESLGSSGHGV SHLAIGIGVN LAAAPDPAGI EPTTAPPVSV AGETGMAPGP
     EEFLTCLAAA FARWEAQLAT FGFGPIRTAW LARAARLGQT ITARTMTESI EGRFETIDDT
     GALVLVTAQG RRAVPAADVY F
//
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