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Database: UniProt
Entry: R4VHH1_9GAMM
LinkDB: R4VHH1_9GAMM
Original site: R4VHH1_9GAMM 
ID   R4VHH1_9GAMM            Unreviewed;       261 AA.
AC   R4VHH1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=SPISAL_07660 {ECO:0000313|EMBL:AGM41626.1};
OS   Spiribacter salinus M19-40.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Spiribacter.
OX   NCBI_TaxID=1260251 {ECO:0000313|EMBL:AGM41626.1, ECO:0000313|Proteomes:UP000017881};
RN   [1] {ECO:0000313|EMBL:AGM41626.1, ECO:0000313|Proteomes:UP000017881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M19-40 {ECO:0000313|EMBL:AGM41626.1};
RX   PubMed=23409269;
RA   Leon M.J., Ghai R., Fernandez A.B., Sanchez-Porro C., Rodriguez-Valera F.,
RA   Ventosa A.;
RT   "Draft Genome of Spiribacter salinus M19-40, an Abundant
RT   Gammaproteobacterium in Aquatic Hypersaline Environments.";
RL   Genome Announc. 1:E00179-12(2013).
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; CP005963; AGM41626.1; -; Genomic_DNA.
DR   RefSeq; WP_016353933.1; NC_021291.1.
DR   AlphaFoldDB; R4VHH1; -.
DR   KEGG; ssal:SPISAL_07660; -.
DR   PATRIC; fig|1260251.3.peg.1550; -.
DR   eggNOG; COG0340; Bacteria.
DR   HOGENOM; CLU_051096_6_1_6; -.
DR   OrthoDB; 9807064at2; -.
DR   Proteomes; UP000017881; 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   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:AGM41626.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017881}.
FT   DOMAIN          7..188
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   261 AA;  27025 MW;  526E0CD0B73CC20E CRC64;
     MTTQDTLAAV QAGLGPRHAQ TAIHVFESLA STNEWLAAQS LAGPTLVTAR TQTQGRGRRG
     RAWASPAGGW YFSVGVPLSP DEPVQPTVTL LVGIALAEAL TSAGFPGIAV KWPNDLVVNG
     AKLGGILVER LPTALIVGVG INRSTTAIQN LPTDRRAIGL KDLGDRPTHE NLIGQLAAAI
     FDAVMRSPDA AAAILDACWP ARDALAGHIV VVTQSDGTGT PLQGEVLGIT PNGQLRLATA
     SGEQWVNAGE CRIQGGWEAT A
//
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