ID Q1KR72_STRSL Unreviewed; 152 AA.
AC Q1KR72;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=D-alanine:D-alanine ligase {ECO:0000313|EMBL:ABE73667.1};
DE Flags: Fragment;
GN Name=ddlA {ECO:0000313|EMBL:ABE73667.1};
OS Streptococcus salivarius.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1304 {ECO:0000313|EMBL:ABE73667.1};
RN [1] {ECO:0000313|EMBL:ABE73667.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=10 {ECO:0000313|EMBL:ABE73665.1}, 11
RC {ECO:0000313|EMBL:ABE73666.1}, 12 {ECO:0000313|EMBL:ABE73667.1}, 4
RC {ECO:0000313|EMBL:ABE73659.1}, 6 {ECO:0000313|EMBL:ABE73661.1}, and 8
RC {ECO:0000313|EMBL:ABE73663.1};
RX PubMed=17085557; DOI=10.1128/JB.01058-06;
RA Delorme C., Poyart C., Ehrlich S.D., Renault P.;
RT "Extent of horizontal gene transfer in evolution of Streptococci of the
RT salivarius group.";
RL J. Bacteriol. 189:1330-1341(2007).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; DQ460612; ABE73659.1; -; Genomic_DNA.
DR EMBL; DQ460614; ABE73661.1; -; Genomic_DNA.
DR EMBL; DQ460616; ABE73663.1; -; Genomic_DNA.
DR EMBL; DQ460618; ABE73665.1; -; Genomic_DNA.
DR EMBL; DQ460619; ABE73666.1; -; Genomic_DNA.
DR EMBL; DQ460620; ABE73667.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1KR72; -.
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 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABE73667.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 1..152
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABE73667.1"
FT NON_TER 152
FT /evidence="ECO:0000313|EMBL:ABE73667.1"
SQ SEQUENCE 152 AA; 16421 MW; 8DD7DE2C772E8E2C CRC64;
LEVAGVPQVA YTVFIEGEDL EVAVAETLEK LTFPVFVKPA NMGSSVGISK AENEAELRAA
IDLALKYDSR ILIEQGVVAR EIEVGILGNT NVKTTDPGEV VKDVAFYDYQ AKYIDNKITM
DIPAHVPAEV MTQMRAYAAK AFRALGGCGL AR
//
