ID DDL_YERPG Reviewed; 306 AA.
AC A9R122;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 01-MAY-2013, entry version 50.
DE RecName: Full=D-alanine--D-alanine ligase;
DE EC=6.3.2.4;
DE AltName: Full=D-Ala-D-Ala ligase;
DE AltName: Full=D-alanylalanine synthetase;
GN Name=ddl; OrderedLocusNames=YpAngola_A2916;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/JB.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y.,
RA Mou S., Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola
RT reveals new insights into the evolution and pangenome of the plague
RT bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
CC -!- FUNCTION: Cell wall formation (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC alanyl-D-alanine.
CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR EMBL; CP000901; ABX88319.1; -; Genomic_DNA.
DR RefSeq; YP_001607293.1; NC_010159.1.
DR ProteinModelPortal; A9R122; -.
DR SMR; A9R122; 1-306.
DR STRING; 349746.YpAngola_A2916; -.
DR EnsemblBacteria; ABX88319; ABX88319; YpAngola_A2916.
DR GeneID; 5801388; -.
DR KEGG; ypg:YpAngola_A2916; -.
DR PATRIC; 18575353; VBIYerPes97331_3439.
DR eggNOG; COG1181; -.
DR HOGENOM; HOG000011592; -.
DR KO; K01921; -.
DR OMA; EVLVEKW; -.
DR ProtClustDB; PRK01372; -.
DR UniPathway; UPA00219; -.
DR GO; GO:0005618; C:cell wall; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 2.
DR Gene3D; 3.40.50.20; -; 1.
DR HAMAP; MF_00047; Dala_Dala_lig; 1; -.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
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.
DR PANTHER; PTHR23132; PTHR23132; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01820; Dala_Dala_lig_N; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 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; Cell shape; Cell wall biogenesis/degradation;
KW Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Peptidoglycan synthesis.
FT CHAIN 1 306 D-alanine--D-alanine ligase.
FT /FTId=PRO_1000091218.
FT DOMAIN 101 303 ATP-grasp.
FT NP_BIND 134 189 ATP (By similarity).
FT METAL 257 257 Magnesium or manganese 1 (By similarity).
FT METAL 270 270 Magnesium or manganese 1 (By similarity).
FT METAL 270 270 Magnesium or manganese 2 (By similarity).
FT METAL 272 272 Magnesium or manganese 2 (By similarity).
SQ SEQUENCE 306 AA; 33150 MW; C78CFF3D2E11F846 CRC64;
MAEKVAVLLG GTSAEREVSL LSGQAVLAGL KEAGIDAYGV DTKDFPVTQL KEQGFDKVFI
ALHGRGGEDG TLQGVLEFLQ LPYTGSGVMA SALTMDKLRT KLVWQALGLP ISPYVALNRQ
QFETLSPEEL VACVAKLGLP LIVKPSHEGS SVGMSKVDHA SELQKALVEA FQHDSDVLIE
KWLSGPEFTV AILGDEVLPS IRIQPPGVFY DYDAKYLSDK TQYFCPSGLS DESEQQLAAL
ALQAYHALDC SGWGRVDVMQ DRDGHFYLLE VNTSPGMTSH SLVPMAARQY GLSFSQLVAR
ILMLAD
//