ID   D2BEG1_STRRD            Unreviewed;       318 AA.
AC   D2BEG1;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE            EC=6.3.2.4 {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=Sros_9380 {ECO:0000313|EMBL:ACZ91998.1};
OS   Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS   9100).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ91998.1, ECO:0000313|Proteomes:UP000002029};
RN   [1] {ECO:0000313|EMBL:ACZ91998.1, ECO:0000313|Proteomes:UP000002029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC   {ECO:0000313|Proteomes:UP000002029};
RX   PubMed=21304675; DOI=10.4056/sigs.631049;
RA   Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA   Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA   Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA   Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Streptosporangium roseum type strain (NI
RT   9100).";
RL   Stand. Genomic Sci. 2:29-37(2010).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
CC         phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
CC         Evidence={ECO:0000256|HAMAP-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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001814; ACZ91998.1; -; Genomic_DNA.
DR   RefSeq; WP_012895724.1; NC_013595.1.
DR   AlphaFoldDB; D2BEG1; -.
DR   STRING; 479432.Sros_9380; -.
DR   KEGG; sro:Sros_9380; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_1_0_11; -.
DR   OrthoDB; 9813261at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002029; 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:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; 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   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   PIRSF; PIRSF039102; Ddl/VanB; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00047};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00047};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000313|EMBL:ACZ91998.1};
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|PROSITE-ProRule:PRU00409};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002029}.
FT   DOMAIN          103..310
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT   BINDING         277
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT   BINDING         277
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT   BINDING         279
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
SQ   SEQUENCE   318 AA;  32934 MW;  A400422C10F2CC96 CRC64;
     MSDLGYVLVL AGGLSYEREV SLRSGRRVSE VLRTAGIVVE TRDTDASLVP SILADPPDAV
     FVTLHGGAGE DGAIRSVLEL LSVPYVGAGP DACRVAFDKP TAKTVVRSVG LRTPDSVTLP
     KETFHDLGAS TVLTRIVERL GLPLFVKPSR GGSALGASIV RAAEDLPAAM VGCFAYGDTA
     LIERCIEGVE VAVSVVDLGG GPMALPPVEI VPDKGVYDYA ARYTAGHTEF FAPARLSPEA
     AAACAEMAVT AHTALGLRDI SRTDLIVDGD GLPHFLEVNV APGMTETSLL PMAVEAAGDD
     LGTLCRVLLE QAAARGAA
//