ID DDL_RHOJR Reviewed; 368 AA.
AC Q0S2F6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 13-NOV-2019, entry version 97.
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=RHA1_ro06507;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA Davies J.E., Mohn W.W., Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG98280.1; -; Genomic_DNA.
DR RefSeq; WP_009479693.1; NC_008268.1.
DR SMR; Q0S2F6; -.
DR STRING; 101510.RHA1_ro06507; -.
DR PRIDE; Q0S2F6; -.
DR EnsemblBacteria; ABG98280; ABG98280; RHA1_ro06507.
DR GeneID; 4224058; -.
DR KEGG; rha:RHA1_ro06507; -.
DR eggNOG; ENOG4105CPF; Bacteria.
DR eggNOG; COG1181; LUCA.
DR HOGENOM; HOG000011593; -.
DR KO; K01921; -.
DR OMA; NTTPGMT; -.
DR BioCyc; RJOS101510:G1G71-6490-MONOMER; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008710; 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;
KW Reference proteome.
FT CHAIN 1 368 D-alanine--D-alanine ligase.
FT /FTId=PRO_0000341164.
FT DOMAIN 151 358 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_00047}.
FT NP_BIND 179 234 ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 313 313 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 325 325 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 325 325 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 327 327 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ SEQUENCE 368 AA; 38959 MW; 065306718D1597FA CRC64;
MSKPRTRVAV IFGGRSNEHS VSCVSAGSVL RNLDPERYEV VPIGITTEGS WVLGSTDPET
LSIRGRALPS VDADGSALAL TADPTRSGDL VALDDGEAGK ILASVDVVFP VLHGAYGEDG
TIQGLLELAG VPYVGPGVLA SAAGMDKEFT KKLLAAEGLP IGFQVVLRPG TATLTDEQKS
RLHLPVFVKP ARGGSSIGIT RVAEWAALDD AIAHARLHDP KVIVESGIIG REVECGVLEF
PDGDVRASVI AEIRMPEGAG DDEAFYDFDS KYLDDVCEFD VPAKLDESVS DEIRELAVRA
FSALDCQGLA RVDFFVTEDG PVINEINTMP GFTSISMYPR MWGAVGVDYG TLVSTLVDTA
LARGIGLR
//
