ID DDL_VIBC3 Reviewed; 329 AA.
AC A5F083; C3M614;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 05-DEC-2018, entry version 77.
DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047};
DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047};
GN Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047}; Synonyms=ddlA;
GN OrderedLocusNames=VC0395_0515, VC395_A0743;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y.,
RA Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the
RT cholera pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
CC -!- FUNCTION: Cell wall formation. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00047};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000250};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_00047}.
DR EMBL; CP000626; ABQ18505.1; -; Genomic_DNA.
DR EMBL; CP001236; ACP11577.1; -; Genomic_DNA.
DR RefSeq; WP_000169442.1; NC_012583.1.
DR ProteinModelPortal; A5F083; -.
DR SMR; A5F083; -.
DR STRING; 345073.VC0395_0515; -.
DR EnsemblBacteria; ABQ18505; ABQ18505; VC0395_0515.
DR EnsemblBacteria; ACP11577; ACP11577; VC395_A0743.
DR KEGG; vco:VC0395_0515; -.
DR KEGG; vcr:VC395_A0743; -.
DR PATRIC; fig|345073.21.peg.3476; -.
DR eggNOG; ENOG4105CPF; Bacteria.
DR eggNOG; COG1181; LUCA.
DR HOGENOM; HOG000011592; -.
DR KO; K01921; -.
DR OMA; YETKYTE; -.
DR OrthoDB; POG091H06GK; -.
DR BioCyc; VCHO345073:G1GU4-3656-MONOMER; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000249; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 1.
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; Cell shape; Cell wall biogenesis/degradation;
KW Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Peptidoglycan synthesis.
FT CHAIN 1 329 D-alanine--D-alanine ligase.
FT /FTId=PRO_1000074803.
FT DOMAIN 121 327 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_00047}.
FT NP_BIND 151 206 ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 281 281 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 294 294 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 294 294 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 296 296 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ SEQUENCE 329 AA; 36765 MW; 26818B896BF4D810 CRC64;
MTKTTILLLC GGGSSEHEIS LVSANYIQQQ LELTPEFHVI RVEMKKEGWF SEQGALVYLD
TNSATLNSDK ASYPIDFVVP CIHGFPGETG DIQSMLELAG IPYLGCGPEA SANSFNKITS
KLWYDALDIP NTPYLFLTQN TPSSIDKAKQ AFGHWGSIFV KAARQGSSVG CYKVTTEDQI
APAIEAAFGF SEQVLVEQAV KPRELEVSAY EMNGKLYISK PGEVIAPEGT FYSYEEKYSA
NSHARTVLEA ENLTEKHKEL IQTYAERVFI HMKLRHLSRI DFFLTQEGQI YLNEVNTFPG
MTPISMFPKM LEHNGHRFSE FLAQCVTNT
//
