ID   A4CP91_ROBBH            Unreviewed;       329 AA.
AC   A4CP91;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   04-NOV-2026, entry version 118.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|ARBA:ARBA00012216, ECO:0000256|HAMAP-Rule:MF_00047};
DE            EC=6.3.2.4 {ECO:0000256|ARBA:ARBA00012216, ECO:0000256|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
GN   Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=RB2501_02270 {ECO:0000313|EMBL:EAR14212.1};
OS   Robiginitalea biformata (strain ATCC BAA-864 / DSM 15991 / KCTC 12146 /
OS   HTCC2501).
OC   Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Robiginitalea.
OX   NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR14212.1, ECO:0000313|Proteomes:UP000009049};
RN   [1] {ECO:0000313|EMBL:EAR14212.1, ECO:0000313|Proteomes:UP000009049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC   {ECO:0000313|Proteomes:UP000009049};
RX   PubMed=19767438; DOI=10.1128/JB.01191-09;
RA   Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL   J. Bacteriol. 191:7144-7145(2009).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 D-alanine + ATP = D-alanyl-D-alanine + ADP + phosphate +
CC         H(+); Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57416, ChEBI:CHEBI:57822,
CC         ChEBI:CHEBI:456216; EC=6.3.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00047614, ECO:0000256|HAMAP-
CC         Rule:MF_00047};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR039102-3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871, ECO:0000256|HAMAP-Rule:MF_00047}.
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DR   EMBL; CP001712; EAR14212.1; -; Genomic_DNA.
DR   RefSeq; WP_015755648.1; NC_013222.1.
DR   AlphaFoldDB; A4CP91; -.
DR   STRING; 313596.RB2501_02270; -.
DR   KEGG; rbi:RB2501_02270; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_1_1_10; -.
DR   OMA; AACDCRD; -.
DR   OrthoDB; 9813261at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000009049; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.20; -; 1.
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   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR000291; D-Ala_lig_Van_CS.
DR   InterPro; IPR005905; D_ala_D_ala.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1.
DR   NCBIfam; NF002378; PRK01372.1; 1.
DR   NCBIfam; NF002527; PRK01966.1-3; 1.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   PIRSF; PIRSF039102; Ddl/VanB; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00843; DALA_DALA_LIGASE_1; 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};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00047};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00047};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00047};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00047};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR039102-3};
KW   Manganese {ECO:0000256|PIRSR:PIRSR039102-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039102-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00047}; Reference proteome {ECO:0000313|Proteomes:UP000009049}.
FT   DOMAIN          123..322
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   ACT_SITE        17
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-1"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-1"
FT   ACT_SITE        300
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-1"
FT   BINDING         289
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT   BINDING         289
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
SQ   SEQUENCE   329 AA;  36164 MW;  668C4C03D8BAC8E7 CRC64;
     MGSTKKIAVI MGGYSSEYEI SLKSGEVVCK WLDRDQYDPY RILIRRDKWV MLGDSGREYP
     VSRHDFSVEL EDGTLRFDCV FNAIHGTPGE NGLMQAYFEL IGMPQTSCGF YQAAVTFNKR
     DLLGILKSAG VPAARSYHLD RGQELNQQAI LDAVGLPCFV KANRAGSSFG VSLVREASGL
     QAAVENALKE DDEILIEAAL QGTEVSVGVI RYQGATRVLP ITEIVSENDF FDYQAKYEGK
     SREITPARIP EDTAEKVREL AARIYDRLRM TGYSRSEFIL VDGEPHLLEV NTTPGLTEAS
     ILPQQAACAG ISLTELFGSA IADALDKNG
//