ID Q2V247_STRMG Unreviewed; 96 AA.
AC Q2V247;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=D-alanine:D-alanine ligase {ECO:0000313|EMBL:BAE53894.1};
DE Flags: Fragment;
GN Name=ddl {ECO:0000313|EMBL:BAE53894.1};
OS Streptococcus mutans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1309 {ECO:0000313|EMBL:BAE53894.1};
RN [1] {ECO:0000313|EMBL:BAE53894.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1651 {ECO:0000313|EMBL:BAE53894.1};
RX PubMed=16333101; DOI=10.1128/JCM.43.12.6073-6085.2005;
RA Hoshino T., Fujiwara T., Kilian M.;
RT "Use of phylogenetic and phenotypic analyses to identify nonhemolytic
RT streptococci isolated from bacteremic patients.";
RL J. Clin. Microbiol. 43:6073-6085(2005).
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DR EMBL; AB199445; BAE53894.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2V247; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
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; IPR013815; ATP_grasp_subdomain_1.
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.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:BAE53894.1}.
FT DOMAIN 1..96
FT /note="D-alanine--D-alanine ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07478"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAE53894.1"
FT NON_TER 96
FT /evidence="ECO:0000313|EMBL:BAE53894.1"
SQ SEQUENCE 96 AA; 10664 MW; E04D05CFA792E76F CRC64;
AIALALKYDS RVLIEQGVDA REIEVGILGN TDVKTTLPGE IVKDVAFYDY EAKYIDNKIT
MAIPAEIDPV IVEKMRDYAA TAFRTLDCCG LSRCDF
//
