BACD_BACIU
ID BACD_BACIU Reviewed; 472 AA.
AC Q8KWT3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 subtilis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BACILYSIN PRODUCTION, AND
RP GENE NAME.
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 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; AF396778; AAM90571.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KWT3; -.
DR SMR; Q8KWT3; -.
DR STRING; 483913.AN935_19100; -.
DR PATRIC; fig|1423.171.peg.2214; -.
DR BRENDA; 6.3.2.49; 658.
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_0000064802"
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; 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
