ID BACD2_BACSU Reviewed; 472 AA. AC Q8KWT3; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Alanine-anticapsin ligase bacD; DE EC=6.3.2.28; DE AltName: Full=L-amino acid ligase; DE AltName: Full=Bacilysin synthetase; GN Name=bacD; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A1/3; RX PubMed=15609023; DOI=10.1007/s00203-004-0743-8; RA Steinborn G., Hajirezaei M.-R., Hofemeister J.; RT "bac genes for recombinant bacilysin and anticapsin production in RT Bacillus host strains."; RL Arch. Microbiol. 183:71-79(2005). CC -!- FUNCTION: Catalyzes the formation of alpha-dipeptides from various CC L-amino acids in the presence of ATP. Probably catalyzes the CC ligation of L-alanine and L-anticapsin to produce the final CC bacilysin antibiotic (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + an L-amino acid + an L-amino acid = ADP CC + phosphate + L-aminoacyl-L-amino acid. CC -!- COFACTOR: Magnesium or manganese (By similarity). CC -!- PATHWAY: Antibiotic biosynthesis; bacilysin biosynthesis. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF396778; AAM90571.1; -; Genomic_DNA. DR BRENDA; 6.3.2.28; 150. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0034026; F:L-amino-acid alpha-ligase activity; IEA:EC. DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR011761; ATP-grasp. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW Antibiotic biosynthesis; ATP-binding; Ligase; Nucleotide-binding. FT CHAIN 1 472 Alanine-anticapsin ligase bacD. FT /FTId=PRO_0000064802. FT DOMAIN 142 355 ATP-grasp. FT NP_BIND 168 235 ATP (By similarity). SQ SEQUENCE 472 AA; 52166 MW; D39D317DD624E5FC CRC64; MERKTVLVIA DLGGCPPHMF YKSAAEKYNL VSFIPRPFAI TASHAALIEK YSVAVIKDKD YFKSLADFEH PDSIYWAHED HDKPEEEVVE EIVKVAGMFA VDAITTNNEL FIAPMAKACE RLGLRGAGVQ AAENARDKNK MRAAFNRAGV KSIKNKRVTT LEDFRAALQE IGTPLILKPT YLASSIGVTL IKEMETAEAE FNRVNEYLKS INVPKAVTFE APFIAEEFLQ GEYDDWYETS GYSDYISIEG IMADGEYFPV AIHDKTPQIG FTETSHITPS ILDDDAKRKI VEAAKKANEG LGLENCATHT EIKLMKNREA GLIESAARFA GWNMIPNIKK VFGVDMAQLL LDVLCFGKEA DLPKGLLEQE PCYVADCHLY PQHFKENGQL PETAVDFVIE SIDIPDGVLK GDTEIVSFSA AEAGTSVDLR LFEAFNSIAA FELKGSNSGD VAESIKQIQQ QAKLTAKYAL PV //