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Entry: A0A0F6SFE9_9DELT
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ID   A0A0F6SFE9_9DELT        Unreviewed;       366 AA.
AC   A0A0F6SFE9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-NOV-2017, entry version 20.
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   ORFNames=DB32_003973 {ECO:0000313|EMBL:AKF06824.1};
OS   Sandaracinus amylolyticus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Sandaracinaceae; Sandaracinus.
OX   NCBI_TaxID=927083 {ECO:0000313|EMBL:AKF06824.1, ECO:0000313|Proteomes:UP000034883};
RN   [1] {ECO:0000313|EMBL:AKF06824.1, ECO:0000313|Proteomes:UP000034883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 53668 {ECO:0000313|EMBL:AKF06824.1,
RC   ECO:0000313|Proteomes:UP000034883};
RA   Sharma G., Subramanian S.;
RT   "Genome assembly of Sandaracinus amylolyticus DSM 53668.";
RL   Submitted (MAR-2015) 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|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: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; CP011125; AKF06824.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKF06824; AKF06824; DB32_003973.
DR   KEGG; samy:DB32_003973; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000034883; 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:UP000034883};
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:AKF06824.1};
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:UP000034883}.
FT   DOMAIN      141    338       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   METAL       292    292       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       305    305       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       305    305       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       307    307       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ   SEQUENCE   366 AA;  39050 MW;  937E342984D9734D CRC64;
     MARGLRHHPA RPSAANGRGS SIADGRASHG GARRMKSGGK QFGRVGVLMG GLGAERDISL
     ATGEAIAKAL EERGHDVVRV IVDRDVDRVL RQTPIDVAFL ALHGTYGEDG CIQGMLEMMG
     IPYTGSGVLA SALAMDKLKS KELFRLYNVP TPPYYVAESD QLDRLEELHG SFGFPVFVKP
     RRSGSSVGAG KANDMAELRA RCEDAARYDR SILVERFVAG KEVRVAVLDG RALGAIEIVP
     KGEFYDYRSK YSKGRSEYHF PARLAPTRYK GVLTLAERAH RALGCEGATG VDLLVTEGEN
     EYVLEVNTIP GMTPTSLLPK IAAGAGYDFG DLCEAILSRA ALGAPSDAER DEDGAVGDGA
     AVVAAE
//
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