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Database: UniProt/SWISS-PROT
Entry: DDL_SHEWM
LinkDB: DDL_SHEWM
Original site: DDL_SHEWM 
ID   DDL_SHEWM               Reviewed;         335 AA.
AC   B1KI99;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   28-MAR-2018, entry version 61.
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=Swoo_2674;
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32;
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., Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACA86950.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000961; ACA86950.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041418165.1; NC_010506.1.
DR   ProteinModelPortal; B1KI99; -.
DR   SMR; B1KI99; -.
DR   STRING; 392500.Swoo_2674; -.
DR   EnsemblBacteria; ACA86950; ACA86950; Swoo_2674.
DR   KEGG; swd:Swoo_2674; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; RCDFFVI; -.
DR   OrthoDB; POG091H06GK; -.
DR   BioCyc; SWOO392500:G1GBD-2927-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002168; 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-EC.
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-UniPathway.
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;
KW   Reference proteome.
FT   CHAIN         1    335       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341172.
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   335 AA;  37321 MW;  70EA9D910A16C81E CRC64;
     MSQINLLLLC GGGGDEHAIS LMSADFLETS LAKEPEINLL RVELDGQGHY RTQDGRSCEL
     TNRKEIRFAA EEQAPWPVDY VIPCIHGFPG ETGDIQSYFD LIKLPFFGCD SESSSNCFNK
     VTAKMWFSAL GVPNTPYIFL NELNQESIAQ TKQALENWGS IFIKAASQGS SVGCYRVDSQ
     DELVSSLEQA FSFSPYVIVE KTINARELEV AAYELNGEIV ATKPGEIICA SNTFYSFDEK
     YAANSKAETK VEADVSEEVA QQIQAYAIKV FKGMKLSHLS RIDFFLTEDN EILLNEINTF
     PGLTPISMFP KMLQNHGDDF THYLYSNIKS QLVSA
//
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