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Database: UniProt/SWISS-PROT
Entry: DDL_SHEPW
LinkDB: DDL_SHEPW
Original site: DDL_SHEPW 
ID   DDL_SHEPW               Reviewed;         332 AA.
AC   B8CMV8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   17-JUN-2020, entry version 71.
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}; OrderedLocusNames=swp_2771;
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877;
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(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. {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; CP000472; ACJ29498.1; -; Genomic_DNA.
DR   RefSeq; WP_020912852.1; NC_011566.1.
DR   SMR; B8CMV8; -.
DR   STRING; 225849.swp_2771; -.
DR   EnsemblBacteria; ACJ29498; ACJ29498; swp_2771.
DR   KEGG; swp:swp_2771; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; CLU_039268_0_0_6; -.
DR   KO; K01921; -.
DR   OMA; IDFFLTD; -.
DR   OrthoDB; 764798at2; -.
DR   BioCyc; SPIE225849:G1G7F-2532-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000753; 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; Cytoplasm;
KW   Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..332
FT                   /note="D-alanine--D-alanine ligase"
FT                   /id="PRO_1000116638"
FT   DOMAIN          124..329
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT   NP_BIND         154..209
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT   METAL           283
FT                   /note="Magnesium or manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT   METAL           296
FT                   /note="Magnesium or manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT   METAL           296
FT                   /note="Magnesium or manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT   METAL           298
FT                   /note="Magnesium or manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
SQ   SEQUENCE   332 AA;  36871 MW;  75090F64ADEA5C86 CRC64;
     MSTTNILLLC GGGGDEHAIS LLSANYFETS LATLPQFNVL RVELDVNGHY RTAAGESCEL
     NSRRQIRFDA DNRAPWEVDF AIPCIHGFPG ETGDIQSYFE LINLPYFGCK AEASRNCFNK
     ITAKMWFSAL NIPNTPYLFL NEMSDVSIEQ ATNALVNWGS IFVKAASQGS SVGCYRIDNQ
     EDVASTLAQA FTYSDYVIVE KTISARELEV AVYEIDGEIV ATVPGEVICS SNNFYTFDEK
     YAANSKAQTQ VVADISKEVS DLIRQYAISA FKGMKLRHLS RIDFFLTDDG EVLLNEINTF
     PGLTPISMFP KMLQNHGHSF PDYLLSNINS TD
//
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