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D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)

 A0A0L6JBC9_9RHIZ        Unreviewed;       307 AA.
A0A0L6JBC9;
11-NOV-2015, integrated into UniProtKB/TrEMBL.
11-NOV-2015, sequence version 1.
22-NOV-2017, entry version 17.
RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
ORFNames=AKJ13_07605 {ECO:0000313|EMBL:KNY23136.1};
Methylobacterium sp. ARG-1.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Methylobacteriaceae; Methylobacterium.
NCBI_TaxID=1692501 {ECO:0000313|EMBL:KNY23136.1, ECO:0000313|Proteomes:UP000036734};
[1] {ECO:0000313|Proteomes:UP000036734}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ARG-1 {ECO:0000313|Proteomes:UP000036734};
Hirst R., James-Pederson M., Tai A.;
"Draft Genome Sequence of Methylobacterium sp. Strain ARG-1 Isolated
from the White-Rot Fungus, Armillaria gallica.";
Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00910576}.
-!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00910566}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000256|PIRSR:PIRSR039102-3};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|SAAS:SAAS00910564};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910582}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00644680}.
-!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
{ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910642}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KNY23136.1}.
-----------------------------------------------------------------------
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EMBL; LHCD01000005; KNY23136.1; -; Genomic_DNA.
RefSeq; WP_007562331.1; NZ_LHCD01000005.1.
EnsemblBacteria; KNY23136; KNY23136; AKJ13_07605.
PATRIC; fig|1692501.3.peg.5216; -.
UniPathway; UPA00219; -.
Proteomes; UP000036734; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.30.1490.20; -; 1.
HAMAP; MF_00047; Dala_Dala_lig; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR000291; D-Ala_lig_Van_CS.
InterPro; IPR005905; D_ala_D_ala.
InterPro; IPR011095; Dala_Dala_lig_C.
InterPro; IPR011127; Dala_Dala_lig_N.
InterPro; IPR016185; PreATP-grasp_dom_sf.
Pfam; PF07478; Dala_Dala_lig_C; 1.
Pfam; PF01820; Dala_Dala_lig_N; 1.
PIRSF; PIRSF039102; Ddl/VanB; 2.
SUPFAM; SSF52440; SSF52440; 1.
TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
ECO:0000256|SAAS:SAAS00644673};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00644714};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00644792};
Complete proteome {ECO:0000313|Proteomes:UP000036734};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00910562};
Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:KNY23136.1};
Magnesium {ECO:0000256|PIRSR:PIRSR039102-3,
ECO:0000256|SAAS:SAAS00910568};
Manganese {ECO:0000256|PIRSR:PIRSR039102-3,
ECO:0000256|SAAS:SAAS00910578};
Metal-binding {ECO:0000256|PIRSR:PIRSR039102-3,
ECO:0000256|SAAS:SAAS00910590};
Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
ECO:0000256|SAAS:SAAS00644673};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047,
ECO:0000256|SAAS:SAAS00644714}.
DOMAIN 101 301 ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
METAL 251 251 Magnesium or manganese 1.
{ECO:0000256|PIRSR:PIRSR039102-3}.
METAL 268 268 Magnesium or manganese 1.
{ECO:0000256|PIRSR:PIRSR039102-3}.
METAL 268 268 Magnesium or manganese 2.
{ECO:0000256|PIRSR:PIRSR039102-3}.
METAL 270 270 Magnesium or manganese 2.
{ECO:0000256|PIRSR:PIRSR039102-3}.
SEQUENCE 307 AA; 32479 MW; A3F178DB8D37C164 CRC64;
MSKHVAVLLG GTSAEREVSL SSGAACAAAL EGEGFRVTRV DVGPDIASVL TALRPDVAFN
ALHGPDGEDG TIQGLLEILK IPYTHSGVLA SALAMNKERA KTVMRAAGVD VPEGRIVNRF
EAAKNHPLPP PYVVKPIAEG SSVGVIIVRD GRTHPPQILA SEEWTFGEQV LAEPYIAGRE
LTCGVMGDKA LGVIEVKAAT GDWYDYDAKY APGGSVHVLP AELKPNVYQR VQELSLTAHQ
ALGCRGVSRA DLRYDDTPGG TGLLVVLEVN TQPGMTQTSL VPEMAAHAGL GFGELVRWMV
EDASLNR


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