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Entry: A0A1B2I4F2_9BACT
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ID   A0A1B2I4F2_9BACT        Unreviewed;       312 AA.
AC   A0A1B2I4F2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-SEP-2017, entry version 9.
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   ORFNames=BED41_07015 {ECO:0000313|EMBL:ANZ44854.1};
OS   Cloacibacillus porcorum.
OC   Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC   Cloacibacillus.
OX   NCBI_TaxID=1197717 {ECO:0000313|EMBL:ANZ44854.1, ECO:0000313|Proteomes:UP000093044};
RN   [1] {ECO:0000313|EMBL:ANZ44854.1, ECO:0000313|Proteomes:UP000093044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL-84 {ECO:0000313|EMBL:ANZ44854.1,
RC   ECO:0000313|Proteomes:UP000093044};
RA   Looft T., Bayles D.O., Alt D.P.;
RT   "Complete genome of Cloacibacillus porcorum.";
RL   Submitted (AUG-2016) 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; CP016757; ANZ44854.1; -; Genomic_DNA.
DR   RefSeq; WP_066744379.1; NZ_CP016757.1.
DR   EnsemblBacteria; ANZ44854; ANZ44854; BED41_07015.
DR   KEGG; cpor:BED41_07015; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000093044; 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.
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.
DR   PROSITE; PS00844; DALA_DALA_LIGASE_2; 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:UP000093044};
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};
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      101    304       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   METAL       258    258       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       271    271       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       271    271       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       273    273       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ   SEQUENCE   312 AA;  33177 MW;  6CAA6D66395BEEB1 CRC64;
     MKAVVLCGGV SPEREVSLNS GAAVAKALAD FGYEAELCDI ASISEFIKSW PEYHAEGVFI
     ALHGGWGEDG RIQAVLEAFG IPYTGSGPEA CMLSMDKTAA KLIFANAGLP VPSGFIATRG
     EEGRGRAEEY LRKYGKIIVK PNGGGSTVGV TILSDIAGYG AALELAWQSE PKALVEEFIE
     GEEATVPVME SIDGGIFALP AIHIKPKSGF YDYKNKYTSG CTEYICPSDL PAETNDRLAA
     LAVMAHRSLG CRSYSRVDFR VTPEGGLYVL EVNTAPGMTA TSLVPKSAKA YGLSFGEFLD
     EVARFSFAID RG
//
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