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Database: UniProt/TrEMBL
Entry: A0A0D5XUC3_9PSED
LinkDB: A0A0D5XUC3_9PSED
Original site: A0A0D5XUC3_9PSED 
ID   A0A0D5XUC3_9PSED        Unreviewed;       322 AA.
AC   A0A0D5XUC3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   12-SEP-2018, entry version 23.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
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=PCL1606_12080 {ECO:0000313|EMBL:AKA22663.1};
OS   Pseudomonas chlororaphis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=587753 {ECO:0000313|EMBL:AKA22663.1, ECO:0000313|Proteomes:UP000032748};
RN   [1] {ECO:0000313|EMBL:AKA22663.1, ECO:0000313|Proteomes:UP000032748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCL1606 {ECO:0000313|EMBL:AKA22663.1,
RC   ECO:0000313|Proteomes:UP000032748};
RX   PubMed=25679537; DOI=10.1094/MPMI-10-14-0326-FI;
RA   Calderon C.E., Ramos C., de Vicente A., Cazorla F.M.;
RT   "Comparative Genomic Analysis of Pseudomonas chlororaphis PCL1606
RT   Reveals New Insight into Antifungal Compounds Involved in
RT   Biocontrol.";
RL   Mol. Plant Microbe Interact. 28:249-260(2015).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00910576}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00910566}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00910571};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00910564};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910582}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00644680}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910642}.
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DR   EMBL; CP011110; AKA22663.1; -; Genomic_DNA.
DR   RefSeq; WP_045881397.1; NZ_CP011110.1.
DR   EnsemblBacteria; AKA22663; AKA22663; PCL1606_12080.
DR   KEGG; pcz:PCL1606_12080; -.
DR   PATRIC; fig|587753.10.peg.1201; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000032748; 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; 3.30.1490.20; -; 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|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644673};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644718};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644792};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032748};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00910562};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:AKA22663.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910568};
KW   Manganese {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910578};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910590};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644705};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644714}.
FT   DOMAIN      116    311       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   METAL       265    265       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       278    278       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       278    278       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       280    280       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ   SEQUENCE   322 AA;  34211 MW;  9C4F76B4A5441C18 CRC64;
     MTAAYATLFS TLAPQDFGRV AVLFGGKSAE RAVSLKSGNA VLEALLSAGV DAFGIDVGDD
     LLQRLLNEKI DRAFIILHGR GGEDGSMQGL LECLGIPYTG SGILASALAM DKLRTKQVWH
     SLGIPTPRHA VLGSEADCIH AAAELGMPLI VKPAHEGSSI GMAKVNSASE LIDAWKAAST
     YDSQVLVEQW IQGPEFTIAT LRGQVLPPIA LGTPHTFYDY DAKYLASDTQ YRIPCGLDSD
     KEQELMDLTA KACGALGIAG WARADVMQDA DGQFWFLEVN TAPGMTDHSL VPMAARAAGL
     DFQQLVLAIL AESVVRNAEP RG
//
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