ID G9GD56_9BACT Unreviewed; 221 AA.
AC G9GD56;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=D-alanine-D-lactate ligase {ECO:0000313|EMBL:AEU25794.1};
DE Flags: Fragment;
GN Name=vanA {ECO:0000313|EMBL:AEU25794.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:AEU25794.1};
RN [1] {ECO:0000313|EMBL:AEU25794.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21881561; DOI=10.1038/nature10388;
RA D'Costa V.M., King C.E., Kalan L., Morar M., Sung W.W., Schwarz C.,
RA Froese D., Zazula G., Calmels F., Debruyne R., Golding G.B., Poinar H.N.,
RA Wright G.D.;
RT "Antibiotic resistance is ancient.";
RL Nature 477:457-461(2011).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; JN316655; AEU25790.1; -; Genomic_DNA.
DR EMBL; JN316657; AEU25794.1; -; Genomic_DNA.
DR AlphaFoldDB; G9GD56; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR000291; D-Ala_lig_Van_CS.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF25; D-ALANINE--D-ALANINE LIGASE A; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Ligase {ECO:0000313|EMBL:AEU25794.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 15..216
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEU25794.1"
SQ SEQUENCE 221 AA; 23647 MW; D1FAD9056ABDB3F8 CRC64;
DIQSSAICMD KSLAYVVART GGIDTPAFSV LDGADMTVPN ELVYPVFVKP ARSGSSFGVT
RVDRANELDA AISAAREYDG KVLIEQAIFG SEVGCAVLGK GSDLFVGEVD QITLLHGIFR
IHQEAAPEQG SENAVVTVPA DLPAEKREEI RATAKTIYMT LGCEGLARVD MFLQEDGRIV
LNEVNTLPGF TSYSRYPRMM AAAGLGRSEL IDRLISSAMG P
//
