BACD_BACAM
ID BACD_BACAM Reviewed; 472 AA.
AC Q8KWS8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Alanine--anticapsin ligase {ECO:0000250|UniProtKB:P39641};
DE EC=6.3.2.49 {ECO:0000250|UniProtKB:P39641};
DE AltName: Full=ATP-dependent dipeptide ligase {ECO:0000250|UniProtKB:P39641};
DE AltName: Full=Bacilysin synthetase {ECO:0000250|UniProtKB:P39641};
DE AltName: Full=L-Ala-L-amino acid dipeptide ligase {ECO:0000250|UniProtKB:P39641};
DE AltName: Full=L-alanine--L-anticapsin ligase {ECO:0000250|UniProtKB:P39641};
DE AltName: Full=L-amino acid ligase {ECO:0000250|UniProtKB:P39641};
DE Short=Lal {ECO:0000250|UniProtKB:P39641};
GN Name=bacD {ECO:0000303|PubMed:15609023};
OS Bacillus amyloliquefaciens (Bacillus velezensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=1390;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BACILYSIN PRODUCTION, AND
RP GENE NAME.
RC STRAIN=ATCC 15841;
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 Bacillus
RT host strains.";
RL Arch. Microbiol. 183:71-79(2005).
CC -!- FUNCTION: Part of the bacABCDEFG operon responsible for the
CC biosynthesis of bacilysin, an irreversible inactivator of the
CC glutaminase domain of glucosamine synthetase. Catalyzes the formation
CC of alpha-dipeptides from various L-amino acids in the presence of ATP.
CC In vivo catalyzes the ligation of L-alanine and L-anticapsin
CC (epoxycyclohexanonyl-Ala) to produce the final bacilysin antibiotic (L-
CC Ala-L-4S-cyclohexenonyl-Ala dipeptide). {ECO:0000250|UniProtKB:P39641}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + L-anticapsin = ADP + bacilysin + H(+) +
CC phosphate; Xref=Rhea:RHEA:44332, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:84310, ChEBI:CHEBI:84311, ChEBI:CHEBI:456216;
CC EC=6.3.2.49; Evidence={ECO:0000250|UniProtKB:P39641};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P39641};
CC Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000250|UniProtKB:P39641};
CC -!- PATHWAY: Antibiotic biosynthesis; bacilysin biosynthesis.
CC {ECO:0000305|PubMed:15609023}.
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000250|UniProtKB:P39641}.
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DR EMBL; AF396779; AAM90576.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KWS8; -.
DR SMR; Q8KWS8; -.
DR STRING; 692420.BAMF_3604; -.
DR eggNOG; COG0151; Bacteria.
DR BRENDA; 6.3.2.49; 630.
DR UniPathway; UPA00100; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034026; F:L-amino-acid alpha-ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; ATP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..472
FT /note="Alanine--anticapsin ligase"
FT /id="PRO_0000064803"
FT DOMAIN 142..355
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 184..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 226..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 309..311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT BINDING 328..331
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P39641"
FT SITE 332
FT /note="Plays a key role in restricting the N-terminal
FT substrate specificity to small amino acids such as L-Ala"
FT /evidence="ECO:0000250|UniProtKB:P39641"
SQ SEQUENCE 472 AA; 52338 MW; 85E4AEE6142428A0 CRC64;
MERKTVLVIA DLGGCPPHMF YESAAEKYNL VSFIPRPFAI TASHAALIEK YSIAVIKDKD
YFKSLADFEH PDSIYWAHED HDKPEEEVVE EIVKVADMFA VDAITTNNEL FIAPMAKACK
RLGLRGAGVQ AAENARDKNK MRAAFNRAGV KSIKNKRVTT LEDFRAALQE IGTPLILKPT
YLASSIGVTL IKEMETAEAE FNRVNEYLKS INVPKAVTFE APFIAEEFLQ GEYDDWYETS
GYSDYISIEG IMADGEYFPV AIHDKTPQIG FTETAHITPS ILDDDAKRKI VEAAKKANEG
LGLENCATHT EIKLMKNREA GLIESAPRFA GWNMIPNIKK VFGVDMAQLL LDVLCFGKEA
DLPKGLLEQE PCYVADCHLY PQHFKENGQL PETVVDFVIE SIEIPDGVLK GDTELVSFSA
AEAGTSVDLR LFEAFNSIAA FELKGSNSND VAESIKQIQQ QAKLTAKYAL SV
