ID A0A0M3QGA7_9DELT Unreviewed; 308 AA.
AC A0A0M3QGA7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 28-FEB-2018, entry version 18.
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 ECO:0000313|EMBL:ALC17649.1};
GN ORFNames=DSOUD_2921 {ECO:0000313|EMBL:ALC17649.1};
OS Desulfuromonas soudanensis.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Desulfuromonas.
OX NCBI_TaxID=1603606 {ECO:0000313|EMBL:ALC17649.1, ECO:0000313|Proteomes:UP000057158};
RN [1] {ECO:0000313|EMBL:ALC17649.1, ECO:0000313|Proteomes:UP000057158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WTL {ECO:0000313|EMBL:ALC17649.1,
RC ECO:0000313|Proteomes:UP000057158};
RA Badalamenti J.P., Summers Z.M., Gralnick J.A., Bond D.R.;
RT "Isolation and Genomic Characterization of a Novel Halophilic Metal-
RT Reducing Deltaproteobacterium from the Deep Subsurface.";
RL Submitted (JUL-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; CP010802; ALC17649.1; -; Genomic_DNA.
DR RefSeq; WP_053551645.1; NZ_CP010802.1.
DR EnsemblBacteria; ALC17649; ALC17649; DSOUD_2921.
DR KEGG; des:DSOUD_2921; -.
DR PATRIC; fig|1603606.3.peg.3149; -.
DR KO; K01921; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000057158; 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.
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:UP000057158};
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:ALC17649.1};
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:UP000057158}.
FT DOMAIN 107 302 ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT METAL 257 257 Magnesium or manganese 1.
FT {ECO:0000256|PIRSR:PIRSR039102-3}.
FT METAL 269 269 Magnesium or manganese 1.
FT {ECO:0000256|PIRSR:PIRSR039102-3}.
FT METAL 269 269 Magnesium or manganese 2.
FT {ECO:0000256|PIRSR:PIRSR039102-3}.
FT METAL 271 271 Magnesium or manganese 2.
FT {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ SEQUENCE 308 AA; 33330 MW; 430E6BF12D22B498 CRC64;
MTREELKSKK IAVLMGGRSA EREISLRTGK AVLGALQGAG YRAVAIDAGR DLAARLTAEE
VEVAFIALHG RYGEDGTVQG MLEMMDIPYT GSGVMASSVA MDKVATKKLL LYHELPTPGF
LPFFRGGDLE ALVQDCRHFP LVVKPAREGS TIGVHIVQDA EGLRRGVAEA LEHDDLLLVE
DYIRGMEITV GVLDDQALPI IQVAPKGGFY DFHAKYTAGQ TEYILPALLD AQVYGRIQEA
AVSACRILGC RGAARVDFMV REREFYCLEV NTIPGMTETS LLPKAAAHAG ISFGELTLRI
LEGAGLHK
//
