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Database: UniProt/TrEMBL
Entry: D3PBV7_DEFDS
LinkDB: D3PBV7_DEFDS
Original site: D3PBV7_DEFDS 
ID   D3PBV7_DEFDS            Unreviewed;       291 AA.
AC   D3PBV7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-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=ddlA {ECO:0000313|EMBL:BAI80080.1};
GN   Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=DEFDS_0598 {ECO:0000313|EMBL:BAI80080.1};
OS   Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS   SSM1).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Deferribacteraceae; Deferribacter.
OX   NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI80080.1, ECO:0000313|Proteomes:UP000001520};
RN   [1] {ECO:0000313|EMBL:BAI80080.1, ECO:0000313|Proteomes:UP000001520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC   {ECO:0000313|Proteomes:UP000001520};
RX   PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA   Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA   Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA   Takai K.;
RT   "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT   the genome sequence of the thermophilic bacterium Deferribacter
RT   desulfuricans SSM1.";
RL   DNA Res. 17:123-137(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|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; AP011529; BAI80080.1; -; Genomic_DNA.
DR   RefSeq; WP_013007328.1; NC_013939.1.
DR   AlphaFoldDB; D3PBV7; -.
DR   STRING; 639282.DEFDS_0598; -.
DR   KEGG; ddf:DEFDS_0598; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_1_1_0; -.
DR   OMA; NTTPGMT; -.
DR   OrthoDB; 9813261at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001520; 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; 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   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; 2.
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.
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:UP000001520}.
FT   DOMAIN          101..289
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT   BINDING         256
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT   BINDING         256
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT   BINDING         258
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
SQ   SEQUENCE   291 AA;  32355 MW;  DD43CE77A6F5EBDE CRC64;
     MYRKIAVLCG GLSSEREVSL KTGEAVKQAL DNLGYDAFLI DVDNNVDKKI RETQPDYCFI
     ALHGKYGEDG SIQGLLEVLG IPYNGAGVAA SAIAYDKHLT KVLVQSVGIK TPDYYLCEND
     KDIRFLPAVV KPAREGSTIG ISIVKSKDEF SKAFSEAKKY DSRVLIERFI EGKELTVGII
     NNEVLPTIYI KPIKGFYDYE SKYTKGMTEY IFETGLNVDE TDKLNNISLK VADLIGCSSL
     CRIDYIYDGK EFFLLEVNTI PGMTETSLLP KAAKKAGYDF EKLIDKIIKG D
//
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