ASL_ENTFU
ID ASL_ENTFU Reviewed; 421 AA.
AC H8L902;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=D-aspartate ligase;
DE EC=6.3.1.12;
DE AltName: Full=Asl(fm);
DE AltName: Full=UDP-MurNAc-pentapeptide:D-aspartate ligase;
GN OrderedLocusNames=EFAU004_01690;
OS Enterococcus faecium (strain Aus0004).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1155766;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aus0004;
RX PubMed=22366422; DOI=10.1128/jb.00259-12;
RA Lam M.M., Seemann T., Bulach D.M., Gladman S.L., Chen H., Haring V.,
RA Moore R.J., Ballard S., Grayson M.L., Johnson P.D., Howden B.P.,
RA Stinear T.P.;
RT "Comparative analysis of the first complete Enterococcus faecium genome.";
RL J. Bacteriol. 194:2334-2341(2012).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION, FUNCTION, CATALYTIC
RP ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, AND PATHWAY.
RC STRAIN=D359;
RX PubMed=16510449; DOI=10.1074/jbc.m600114200;
RA Bellais S., Arthur M., Dubost L., Hugonnet J.E., Gutmann L.,
RA van Heijenoort J., Legrand R., Brouard J.P., Rice L., Mainardi J.L.;
RT "Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic
RT acid onto the peptidoglycan precursor of Enterococcus faecium.";
RL J. Biol. Chem. 281:11586-11594(2006).
CC -!- FUNCTION: Catalyzes the addition of D-aspartate onto the lysine residue
CC in the peptidoglycan precursor UDP-MurNAc-pentapeptide. The ligation
CC occurs between the beta-carboxylate of D-Asp and the epsilon-amino
CC group of L-Lys. Is highly specific for D-aspartate, as L-aspartate, D-
CC glutamate, D-alanine, D-iso-asparagine and D-malate are not substrates.
CC {ECO:0000269|PubMed:16510449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-
CC D-Ala)](n) + n ATP + n D-aspartate = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-
CC L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + n ADP + n
CC H(+) + n phosphate; Xref=Rhea:RHEA:10752, Rhea:RHEA-COMP:14481,
CC Rhea:RHEA-COMP:14482, ChEBI:CHEBI:15378, ChEBI:CHEBI:29990,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:76539,
CC ChEBI:CHEBI:140312, ChEBI:CHEBI:456216; EC=6.3.1.12;
CC Evidence={ECO:0000269|PubMed:16510449};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:16510449};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000305|PubMed:16510449};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000269|PubMed:16510449}.
CC -!- MISCELLANEOUS: The substrate D-aspartate is provided by the coexpressed
CC aspartate racemase, whose gene is adjacent to that of the D-aspartate
CC ligase.
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DR EMBL; CP003351; AFC63774.1; -; Genomic_DNA.
DR AlphaFoldDB; H8L902; -.
DR KEGG; efc:EFAU004_01690; -.
DR HOGENOM; CLU_054906_0_0_9; -.
DR OMA; DIKYDPR; -.
DR BioCyc; EFAE1155766:G1H3H-1784-MON; -.
DR UniPathway; UPA00219; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034025; F:D-aspartate ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR011761; ATP-grasp.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell shape; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Peptidoglycan synthesis.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..421
FT /note="D-aspartate ligase"
FT /id="PRO_0000418973"
FT DOMAIN 130..332
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 161..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 421 AA; 49581 MW; 7B93FCC2F61D0039 CRC64;
MMNSIENEEF IPILLGSDMN VYGMARSFNE AYGKICQAYA SDQLAPTRYS KIVNVEVIPG
FDKDPVFIET MLRLAKERYS DKSKKYLLIA CGDGYAELIS QHKQELSEYF ICPYIDYSLF
ERLINKVSFY EVCEEYDLPY PKTLIVREEM LVNGHLEQEL PFEFPVALKP ANSVEYLSVQ
FEGRKKAFIL ETREEFDLIL GRIYEAGYKS EMIVQDFIPG DDSNMRVLNA YVDEDHQVRM
MCLGHPLLED PTPASIGNYV VIMPDYNEKI YQTIKAFLEK IEYTGFANFD MKYDPRDGEY
KLFEINLRQG RSSFFVTLNG LNLARFVTED RVFNKPFVET TYGTNQSDKA RLWMGVPKKI
FLEYARENED KKLAEQMIKE NRYGTTVFYE KDRSIKRWLL MKYMFHNYIP RFKKYFHVKE
G
