ID DDL_STRZT Reviewed; 347 AA.
AC C1CST6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 01-MAY-2013, entry version 35.
DE RecName: Full=D-alanine--D-alanine ligase;
DE EC=6.3.2.4;
DE AltName: Full=D-Ala-D-Ala ligase;
DE AltName: Full=D-alanylalanine synthetase;
GN Name=ddl; OrderedLocusNames=SPT_1610;
OS Streptococcus pneumoniae (strain Taiwan19F-14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=487213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Taiwan19F-14;
RA Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.;
RT "Complete genome sequence of Streptococcus pneumoniae strain
RT Taiwan19F-14.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC alanyl-D-alanine.
CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR EMBL; CP000921; ACO23289.1; -; Genomic_DNA.
DR RefSeq; YP_002743008.1; NC_012469.1.
DR ProteinModelPortal; C1CST6; -.
DR STRING; 487213.SPT_1610; -.
DR EnsemblBacteria; ACO23289; ACO23289; SPT_1610.
DR GeneID; 7686678; -.
DR KEGG; snt:SPT_1610; -.
DR PATRIC; 19712429; VBIStrPne22502_1658.
DR eggNOG; COG1181; -.
DR HOGENOM; HOG000011593; -.
DR KO; K01921; -.
DR OMA; LLHGPFG; -.
DR ProtClustDB; PRK01966; -.
DR UniPathway; UPA00219; -.
DR GO; GO:0005618; C:cell wall; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA: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; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 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.
FT CHAIN 1 347 D-alanine--D-alanine ligase.
FT /FTId=PRO_1000189750.
FT DOMAIN 131 333 ATP-grasp.
FT NP_BIND 161 216 ATP (By similarity).
FT METAL 287 287 Magnesium or manganese 1 (By similarity).
FT METAL 300 300 Magnesium or manganese 1 (By similarity).
FT METAL 300 300 Magnesium or manganese 2 (By similarity).
FT METAL 302 302 Magnesium or manganese 2 (By similarity).
SQ SEQUENCE 347 AA; 38687 MW; CB05996D46DD9EDA CRC64;
MKQTIILLYG GRSAEREVSV LSAESVMRAV NYDRFTVKTF FISQSGDFIK TQEFSHAPGQ
EDRLMTNETI DWDKKVAPSA IYEEGAVVFP VLHGPMGEDG SVQGFLEVLK MPYVGCNILS
SSLAMDKITT KRVLESAGIA QVPYVAIVEG DDVTAKIAEV EEKLAYPVFT KPSNMGSSVG
ISKSENQEEL RPALELAFRY DSRVLVEQGV NAREIEVGLL GNYDVKSTLP GEVVKDVAFY
DYDAKYIDNK ITMDIPAKIS DDVVAVMRQN AETAFRAIGG LGLSRCDFFY TDKGEIFLNE
LNTMPGFTQW SMYPLLWDNM GISYPELIER LVDLAKESFD KREAHLI
//
