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Database: UniProt
Entry: W0BE09_9GAMM
LinkDB: W0BE09_9GAMM
Original site: W0BE09_9GAMM 
ID   W0BE09_9GAMM            Unreviewed;       278 AA.
AC   W0BE09;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Biotin-[acetyl-CoA-carboxylase] ligase region {ECO:0000313|EMBL:AHE66654.1};
DE            EC=6.3.4.15 {ECO:0000313|EMBL:AHE66654.1};
GN   Name=birA {ECO:0000313|EMBL:AHE66654.1};
GN   ORFNames=Loa_01098 {ECO:0000313|EMBL:AHE66654.1};
OS   Legionella oakridgensis ATCC 33761 = DSM 21215.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE66654.1, ECO:0000313|Proteomes:UP000018838};
RN   [1] {ECO:0000313|EMBL:AHE66654.1, ECO:0000313|Proteomes:UP000018838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR-10, ATCC 33761 {ECO:0000313|Proteomes:UP000018838};
RX   PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003;
RA   Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N.,
RA   Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., Luck C.,
RA   Heuner K.;
RT   "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic
RT   characterization reveals its replication capacity in amoebae.";
RL   Int. J. Med. Microbiol. 303:514-528(2013).
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DR   EMBL; CP004006; AHE66654.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0BE09; -.
DR   STRING; 1268635.Loa_01098; -.
DR   KEGG; lok:Loa_01098; -.
DR   PATRIC; fig|1268635.3.peg.1103; -.
DR   eggNOG; COG0340; Bacteria.
DR   eggNOG; COG1654; Bacteria.
DR   HOGENOM; CLU_051096_4_0_6; -.
DR   Proteomes; UP000018838; 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; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR00121; birA_ligase; 1.
DR   PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR   PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF08279; HTH_11; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AHE66654.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018838}.
FT   DOMAIN          71..262
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   278 AA;  31242 MW;  0119980437680ADA CRC64;
     MKKFSPTQIN LLKELADGLC HSGNHLGLTL GISRTAVWKQ IRQMTDLGVP IATVPQQGYR
     LITPIILLDE ACIRQALSNH DFHLPLNFHL FASIDSTNRF LKELPEHSTL GICCAEQQTQ
     GRGRFGRHWH SPFGENIYFS SRWQFDCDLS QLSGMSLVVS LAILASLNEL GIDDKIGVKW
     PNDLLWQGKK LCGSLIEISA ESNGKTDVVI GIGLNVNSIT EHQPPLEKPW CSLYDITGKP
     WDRNRLIAQL IIQLHAFLQR FLTHGFSFFK SNGNRQTA
//
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