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Database: UniProt/TrEMBL
Entry: A0A0B2XEA7_LACCU
LinkDB: A0A0B2XEA7_LACCU
Original site: A0A0B2XEA7_LACCU 
ID   A0A0B2XEA7_LACCU        Unreviewed;       350 AA.
AC   A0A0B2XEA7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-SEP-2017, entry version 22.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754435};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754435};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
GN   Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047,
GN   ECO:0000313|EMBL:SMH69514.1};
GN   ORFNames=BCY75_00755 {ECO:0000313|EMBL:ANY12665.1}, LCUFL03_380126
GN   {ECO:0000313|EMBL:SMH69514.1}, OA78_0577
GN   {ECO:0000313|EMBL:KHO13338.1};
OS   Lactobacillus curvatus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=28038 {ECO:0000313|EMBL:KHO13338.1, ECO:0000313|Proteomes:UP000031010};
RN   [1] {ECO:0000313|EMBL:KHO13338.1, ECO:0000313|Proteomes:UP000031010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRIC0822 {ECO:0000313|EMBL:KHO13338.1,
RC   ECO:0000313|Proteomes:UP000031010};
RX   PubMed=25501479;
RA   Cousin F.J., Lynch S.M., Harris H.M., McCann A., Lynch D.B.,
RA   Neville B.A., Irisawa T., Okada S., Endo A., O'Toole P.W.;
RT   "Detection and genomic characterization of motility in Lactobacillus
RT   curvatus: confirmation of motility in a species outside the
RT   Lactobacillus salivarius clade.";
RL   Appl. Environ. Microbiol. 0:0-0(2014).
RN   [2] {ECO:0000313|EMBL:ANY12665.1, ECO:0000313|Proteomes:UP000092936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WiKim52 {ECO:0000313|EMBL:ANY12665.1,
RC   ECO:0000313|Proteomes:UP000092936};
RA   Jung M.Y., Lee S.H., Lee J.-H.;
RT   "Complete genome sequence of Lactobacillus curvatus WiKim52.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SMH69514.1, ECO:0000313|Proteomes:UP000193375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FLEC03 {ECO:0000313|EMBL:SMH69514.1};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00754456}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00754451}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR039102-3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00754454};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00644680}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00644812}.
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DR   EMBL; CP016602; ANY12665.1; -; Genomic_DNA.
DR   EMBL; JTJV01000012; KHO13338.1; -; Genomic_DNA.
DR   EMBL; FXDK01000032; SMH69514.1; -; Genomic_DNA.
DR   RefSeq; WP_039098404.1; NZ_MKDG01000009.1.
DR   EnsemblBacteria; ANY12665; ANY12665; BCY75_00755.
DR   EnsemblBacteria; KHO13338; KHO13338; OA78_0577.
DR   KEGG; lcv:FBA2_00250; -.
DR   PATRIC; fig|28038.10.peg.487; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000031010; Unassembled WGS sequence.
DR   Proteomes; UP000092936; Chromosome.
DR   Proteomes; UP000193375; Chromosome lcufl03.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644673};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644718};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644792};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031010,
KW   ECO:0000313|Proteomes:UP000092936, ECO:0000313|Proteomes:UP000193375};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00754427};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:KHO13338.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00754439};
KW   Manganese {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00754447};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00754442};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644705};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644714}.
FT   DOMAIN      146    341       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   METAL       295    295       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       308    308       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       308    308       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       310    310       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ   SEQUENCE   350 AA;  38213 MW;  DD63B42289769E59 CRC64;
     MKIVVLAGGR STERNVSLTS GHKITNALQT KGHDVAFVDL FLGNDLHDVA SIDDLYSSTP
     VEKDYDISDE VLTDDAINAL RTDGSTQLFG PNVLEICKTA DIVFLALHGG DGEDGKVQAV
     LDLFGIPYTG SDTLAAGITM SKKVSKEILL YNQIPTARFV AAYRDQPMPE IPFEYPVVVK
     PSNGGSSVGT HIVHNEAELQ PAVEDALRFD REALIEEFIK GREFSLGVIN GQPLPAIEIV
     VNDGWYDFEH KFVTGNTTQF VTPPNDLPDD VHEAMKQMAL DAMQALGLTN YARIDFFWSP
     ENGLHVIEGN TLPGMTPLSL IPQEAEVLGI SYPDLCEMIV QGKLELLKAK
//
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