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Database: UniProt/TrEMBL
Entry: F6DKQ4_DESRL
LinkDB: F6DKQ4_DESRL
Original site: F6DKQ4_DESRL 
ID   F6DKQ4_DESRL            Unreviewed;       318 AA.
AC   F6DKQ4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   12-SEP-2018, entry version 53.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
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   OrderedLocusNames=Desru_2179 {ECO:0000313|EMBL:AEG60429.1};
OS   Desulfotomaculum ruminis (strain ATCC 23193 / DSM 2154 / NCIB 8452 /
OS   DL).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=696281 {ECO:0000313|EMBL:AEG60429.1, ECO:0000313|Proteomes:UP000009234};
RN   [1] {ECO:0000313|Proteomes:UP000009234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC   {ECO:0000313|Proteomes:UP000009234};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Stams A.J.M.,
RA   Plugge C.M., Muyzer G., Kuever J., Parshina S.N., Ivanova A.E.,
RA   Nazina T.N., Brambilla E., Spring S., Klenk H.-P., Woyke T.;
RT   "Complete sequence of Desulfotomaculum ruminis DSM 2154.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00910576}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00910566}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00910571};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00910564};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910582}.
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:SAAS00910642}.
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DR   EMBL; CP002780; AEG60429.1; -; Genomic_DNA.
DR   RefSeq; WP_013842189.1; NC_015589.1.
DR   EnsemblBacteria; AEG60429; AEG60429; Desru_2179.
DR   KEGG; dru:Desru_2179; -.
DR   KO; K01921; -.
DR   OMA; MQGLLEC; -.
DR   OrthoDB; POG091H00GT; -.
DR   BioCyc; DRUM696281:G1GY6-2219-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000009234; Chromosome.
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_sf.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   PIRSF; PIRSF039102; Ddl/VanB; 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.
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:UP000009234};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00910562};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:AEG60429.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910568};
KW   Manganese {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910578};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910590};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009234}.
FT   DOMAIN      102    307       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   METAL       262    262       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       274    274       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       274    274       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       276    276       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ   SEQUENCE   318 AA;  34356 MW;  704F76A0C534BB64 CRC64;
     MSLCIGVLYG GRSAEREVSL NSGEAVYQAL VAAGYKKVVK IDVGYDLVEQ LKAQKVELAF
     PVLHGKYGED GTLQGLLEMM DIPYTGSGVL SSALAMNKIV TKKIFTLEGI PTPDFTVVTR
     RQVLDQGLEA VAKEALAKMG VPVVVKANTQ GSTIGISFVH KEEEMASAIE SALKYDSDVL
     IEEYIEGMEV TASILGNENP VALPLIEITS VTGVYDYQAK YTPGMSHHII PPGLPEEVQE
     KIKNLAVRAF QSLGCRGLGR VDFMVGEKGI YTLEINTLPG MTGTSLFPDA ARYAGIEFPE
     VADRLVKLAL EFNKHQPG
//
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