ID DDL_SHEHH Reviewed; 333 AA.
AC B0TRK1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 05-DEC-2018, entry version 67.
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};
GN OrderedLocusNames=Shal_1854;
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000931; ABZ76419.1; -; Genomic_DNA.
DR RefSeq; WP_012276951.1; NC_010334.1.
DR ProteinModelPortal; B0TRK1; -.
DR SMR; B0TRK1; -.
DR STRING; 458817.Shal_1854; -.
DR PRIDE; B0TRK1; -.
DR EnsemblBacteria; ABZ76419; ABZ76419; Shal_1854.
DR KEGG; shl:Shal_1854; -.
DR eggNOG; ENOG4105CPF; Bacteria.
DR eggNOG; COG1181; LUCA.
DR HOGENOM; HOG000011592; -.
DR KO; K01921; -.
DR OMA; VFLTPDN; -.
DR OrthoDB; POG091H06GK; -.
DR BioCyc; SHAL458817:G1GB1-1938-MONOMER; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001317; Chromosome.
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 1 333 D-alanine--D-alanine ligase.
FT /FTId=PRO_1000074788.
FT DOMAIN 124 329 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_00047}.
FT NP_BIND 154 209 ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 283 283 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 296 296 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 296 296 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 298 298 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ SEQUENCE 333 AA; 37583 MW; 8897FB4F2AC845B8 CRC64;
MTQKNLLLLC GGGGDEHSIS LLSANFFETQ LATLPHFNVL RVELNAKGQY RTQAGELCEL
TNSKQIRFND QSKAPWDVDY VIPCIHGYPG ETGDIQSYFE LINLPYFGCD SEASSNCFNK
VTAKMWFSAL GIRNTPYIFL NEFNQQAIEE TERALEKWGS IFIKAASQGS SVGCYRVDNK
EQLANSLEEA FKYSPYVVVE KTINARELEV AAYEVDGEII ATKPGEIICA SNTFYSFDEK
YAENSQAQTV IEADVDEVIA KQIQEYAIKA FKGMKLRHLS RIDFFLTDEN EILLNEINTF
PGQTQISMFP KMLQNHGHNF AQYLSGNIMA QLK
//
