ID DDL_VIBCB Reviewed; 329 AA.
AC A7N512;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 26-FEB-2020, entry version 80.
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=VIBHAR_05785;
OS Vibrio campbellii (strain ATCC BAA-1116 / BB120).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=338187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) 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. {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; CP000790; ABU73679.1; -; Genomic_DNA.
DR RefSeq; WP_012129370.1; NC_022270.1.
DR SMR; A7N512; -.
DR PRIDE; A7N512; -.
DR EnsemblBacteria; ABU73679; ABU73679; VIBHAR_05785.
DR GeneID; 5557281; -.
DR KEGG; vca:M892_22760; -.
DR KEGG; vha:VIBHAR_05785; -.
DR PATRIC; fig|338187.25.peg.4496; -.
DR eggNOG; ENOG4105CPF; Bacteria.
DR eggNOG; COG1181; LUCA.
DR KO; K01921; -.
DR OMA; YNLAGCK; -.
DR OrthoDB; 764798at2; -.
DR BioCyc; VCAM338187:G1HKJ-4557-MONOMER; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008152; Chromosome II.
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..329
FT /note="D-alanine--D-alanine ligase"
FT /id="PRO_1000030519"
FT DOMAIN 120..326
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT NP_BIND 150..205
FT /note="ATP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT METAL 280
FT /note="Magnesium or manganese 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT METAL 293
FT /note="Magnesium or manganese 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT METAL 293
FT /note="Magnesium or manganese 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT METAL 295
FT /note="Magnesium or manganese 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
SQ SEQUENCE 329 AA; 36657 MW; B8C2ADAAAEA3DB70 CRC64;
MIKNILLLCG GGSSEHEISL LSANFVEQQL NLIENVSVTR VEIKNEGWVT NQGELVYLDP
NQKKLCSDNL SLDVDFIVPC IHGFPGETGD IQSMFEIAGI PYLGCGPEAS SNSFNKITSK
LWYDAIGIPN TPYLFLTRND EQAHEQALQA FDKWGKVFVK AARQGSSVGC YSVTNKQSVS
QAVNDAFGYS EQVLVEKSVK PRELEVAAYE MNGELHITKP GEVIAPDGAF YSYDEKYSTS
SHSLTEVEAK NLTEEQVEAI RVASETVFKQ MNLRHLSRID FFLTEDGEIY LNEVNTFPGM
TPISMFPKML QNNGHKFHEF LADCINTAI
//
