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Database: UniProt/SWISS-PROT
Entry: DDL_STRMU
LinkDB: DDL_STRMU
Original site: DDL_STRMU 
ID   DDL_STRMU               Reviewed;         349 AA.
AC   P95803;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   28-FEB-2018, entry version 127.
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=SMU_599;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J.,
RA   Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P.,
RA   Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A.,
RA   Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-303.
RC   STRAIN=ATCC 25175 / DSM 20523 / JCM 5705 / NBRC 13955 / NCIMB 702062 /
RC   NCTC 10449;
RA   Garnier F., Gerbaud G., Courvalin P., Galimand M.;
RL   Submitted (FEB-1997) 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}.
DR   EMBL; AE014133; AAN58338.1; -; Genomic_DNA.
DR   EMBL; U69165; AAB41854.1; -; Genomic_DNA.
DR   RefSeq; NP_721032.1; NC_004350.2.
DR   RefSeq; WP_002352219.1; NC_004350.2.
DR   PDB; 3K3P; X-ray; 2.23 A; A/B=1-349.
DR   PDBsum; 3K3P; -.
DR   ProteinModelPortal; P95803; -.
DR   SMR; P95803; -.
DR   STRING; 210007.SMU_599; -.
DR   EnsemblBacteria; AAN58338; AAN58338; SMU_599.
DR   GeneID; 1029384; -.
DR   KEGG; smu:SMU_599; -.
DR   PATRIC; fig|210007.7.peg.532; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   PhylomeDB; P95803; -.
DR   BioCyc; SMUT210007:G1FZX-588-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   EvolutionaryTrace; P95803; -.
DR   Proteomes; UP000002512; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN         1    349       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000177886.
FT   DOMAIN      133    335       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     163    218       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       289    289       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       302    302       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       302    302       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       304    304       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   CONFLICT    132    132       N -> K (in Ref. 2; AAB41854).
FT                                {ECO:0000305}.
FT   CONFLICT    238    238       D -> V (in Ref. 2; AAB41854).
FT                                {ECO:0000305}.
FT   CONFLICT    273    273       A -> R (in Ref. 2; AAB41854).
FT                                {ECO:0000305}.
FT   STRAND        4     11       {ECO:0000244|PDB:3K3P}.
FT   HELIX        17     30       {ECO:0000244|PDB:3K3P}.
FT   TURN         33     35       {ECO:0000244|PDB:3K3P}.
FT   STRAND       36     43       {ECO:0000244|PDB:3K3P}.
FT   STRAND       49     57       {ECO:0000244|PDB:3K3P}.
FT   HELIX        73     75       {ECO:0000244|PDB:3K3P}.
FT   HELIX        79     82       {ECO:0000244|PDB:3K3P}.
FT   STRAND       88     92       {ECO:0000244|PDB:3K3P}.
FT   TURN         96     98       {ECO:0000244|PDB:3K3P}.
FT   STRAND       99    101       {ECO:0000244|PDB:3K3P}.
FT   HELIX       102    109       {ECO:0000244|PDB:3K3P}.
FT   STRAND      114    116       {ECO:0000244|PDB:3K3P}.
FT   HELIX       119    126       {ECO:0000244|PDB:3K3P}.
FT   HELIX       128    138       {ECO:0000244|PDB:3K3P}.
FT   STRAND      146    150       {ECO:0000244|PDB:3K3P}.
FT   HELIX       155    165       {ECO:0000244|PDB:3K3P}.
FT   STRAND      168    174       {ECO:0000244|PDB:3K3P}.
FT   STRAND      184    188       {ECO:0000244|PDB:3K3P}.
FT   HELIX       189    202       {ECO:0000244|PDB:3K3P}.
FT   STRAND      204    210       {ECO:0000244|PDB:3K3P}.
FT   STRAND      214    226       {ECO:0000244|PDB:3K3P}.
FT   STRAND      233    235       {ECO:0000244|PDB:3K3P}.
FT   STRAND      255    258       {ECO:0000244|PDB:3K3P}.
FT   HELIX       263    279       {ECO:0000244|PDB:3K3P}.
FT   STRAND      284    292       {ECO:0000244|PDB:3K3P}.
FT   STRAND      298    306       {ECO:0000244|PDB:3K3P}.
FT   HELIX       314    321       {ECO:0000244|PDB:3K3P}.
FT   HELIX       326    345       {ECO:0000244|PDB:3K3P}.
SQ   SEQUENCE   349 AA;  38838 MW;  FFDAAD9942CAE7EF CRC64;
     MSKETLVLLY GGRSAERDVS VLSAESVMRA INYDNFLVKT YFITQAGDFI KTQEFDSQPS
     ETDKLMTNDT IIASQKIKPS DIYEEEAVVF PVLHGPMGED GSIQGFLEVL KMPYVGTNIL
     SSSVAMDKIT TNQVLESATT IPQVAYVALI EGEPLESKLA EVEEKLIYPV FVKPANMGSS
     VGISKAENRT DLKQAIALAL KYDSRVLIEQ GVDAREIEVG ILGNTDVKTT LPGEIVKDVA
     FYDYEAKYID NKITMAIPAE IDPVIVEKMR DYAATAFRTL GCCGLSRCDF FLTEDGKVYL
     NELNTMPGFT QWSMYPLLWE NMGLSYSVLI EELVSLAKEM FDKRESHLV
//
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