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Database: UniProt
Entry: A4G8T6
LinkDB: A4G8T6
Original site: A4G8T6 
ID   DDL_HERAR               Reviewed;         334 AA.
AC   A4G8T6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   26-NOV-2014, entry version 60.
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=HEAR2809;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M.,
RA   Leize E., Lieutaud A., Lievremont D., Makita Y., Mangenot S.,
RA   Nitschke W., Ortet P., Perdrial N., Schoepp B., Siguier P.,
RA   Simeonova D.D., Rouy Z., Segurens B., Turlin E., Vallenet D.,
RA   van Dorsselaer A., Weiss S., Weissenbach J., Lett M.-C., Danchin A.,
RA   Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-
RT   rich environments.";
RL   PLoS Genet. 3:518-530(2007).
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}.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00047}.
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DR   EMBL; CU207211; CAL62923.1; -; Genomic_DNA.
DR   RefSeq; WP_011872179.1; NC_009138.1.
DR   RefSeq; YP_001101044.1; NC_009138.1.
DR   ProteinModelPortal; A4G8T6; -.
DR   STRING; 204773.HEAR2809; -.
DR   PRIDE; A4G8T6; -.
DR   EnsemblBacteria; CAL62923; CAL62923; HEAR2809.
DR   GeneID; 4930494; -.
DR   KEGG; har:HEAR2809; -.
DR   PATRIC; 22115568; VBIHerArs17568_2642.
DR   eggNOG; COG1181; -.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; ANDTQYR; -.
DR   OrthoDB; EOG6ND0KB; -.
DR   BioCyc; HARS204773:GJCA-2702-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 2.
DR   Gene3D; 3.40.50.20; -; 1.
DR   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
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   PANTHER; PTHR23132; PTHR23132; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 2.
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    334       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341110.
FT   DOMAIN      111    315       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     141    196       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       268    268       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       282    282       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       282    282       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       284    284       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   334 AA;  35913 MW;  D433204BAAE28691 CRC64;
     MTTTVQNLKA EFGKVGVLFG GRSAEREVSL MSGKGVLAAL QSKGVDAHAF DPAERSLAEL
     AAEKFDRVFI ALHGSYGEDG TLQGALEQLG IPYTGPGVMA SAISMDKVMT KRVCLSHGVP
     TPRFTVLDAE TTSAAQLQSV AAEFGLPLML KAPHEGSTIG IAKVETAEGM QAGFDLCAKY
     EAVVLVEQFV KGRELTVPVI GSGRNARALP IVEIRAPQGN YDYEHKYFSN DTEYLCPAPF
     DEAFTKRVQA LAVSAFNAVG CTGWSRVDFM VRASDNEPFL LEINTSPGMT SHSLVPMSAK
     VAGTGYEDLC IEILRSAKTE LKPSSHMQLQ EQER
//
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