ID   A0A5C4UWN0_9ACTN        Unreviewed;       318 AA.
AC   A0A5C4UWN0;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   02-JUN-2021, entry version 5.
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   ORFNames=FH608_049945 {ECO:0000313|EMBL:KAB8182633.1}, FH608_49935
GN   {ECO:0000313|EMBL:TNM27329.1};
OS   Nonomuraea phyllanthi.
OC   Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae;
OC   Nonomuraea.
OX   NCBI_TaxID=2219224 {ECO:0000313|EMBL:TNM27329.1};
RN   [1] {ECO:0000313|EMBL:TNM27329.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA1-10 {ECO:0000313|EMBL:TNM27329.1};
RA   Klykleung N., Kudo T., Yuki M., Ohkuma M., Phongsopitanun W.,
RA   Pittayakhajonwut P., Tanasupawat S.;
RT   "Nonomuraea phyllanthi sp. nov., an endophyte actinomycete isolated from
RT   the leaf of Phyllanthus amarus.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAB8182633.1, ECO:0000313|Proteomes:UP000312512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA1-10 {ECO:0000313|EMBL:KAB8182633.1,
RC   ECO:0000313|Proteomes:UP000312512};
RA   Klykleung N., Tanasupawat S.;
RT   "Nonomuraea sp. nov., isolated from Phyllanthus amarus.";
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_00047}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TNM27329.1}.
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DR   EMBL; VDLX02000040; KAB8182633.1; -; Genomic_DNA.
DR   EMBL; VDLX01000041; TNM27329.1; -; Genomic_DNA.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000312512; Unassembled WGS sequence.
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; 3.30.1490.20; -; 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   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   PIRSF; PIRSF039102; Ddl/VanB; 2.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 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|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:UP000312512}.
FT   DOMAIN          105..310
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   METAL           263
FT                   /note="Magnesium or manganese 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT   METAL           277
FT                   /note="Magnesium or manganese 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT   METAL           277
FT                   /note="Magnesium or manganese 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT   METAL           279
FT                   /note="Magnesium or manganese 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
SQ   SEQUENCE   318 AA;  34662 MW;  57A7200CBD628250 CRC64;
     MTERVRVAVL AGGPSAEHEV SLQSGQAVLE ALPRDLYEPV AVIIDRQGRW PVELRRDLAD
     VVFPVLHGPY GEDGVIQGHL EALGIPYVGC GVLASAVGMN KVAMRRTFLA EDIPVTPHVW
     FTGHEWRTTT DHWGLVKSLD WPMYVKPASM GSSIGISRVT SMEELRAGVD LALAHDRVVI
     VEQGLTAREL ICGVLGGHDT PEASVPGELI VPGDWLDYEA KYLSQAEIAT IPAVLPERVA
     GEVRELSVRA FRAIGGYGLA RVDFLYEEDT GRLYVLEINT MPGFTSRSVY ARAWAASGVP
     YPDLLRRLID LALGRSGS
//