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Database: UniProt/SWISS-PROT
Entry: DDLA_SALTI
LinkDB: DDLA_SALTI
Original site: DDLA_SALTI 
ID   DDLA_SALTI              Reviewed;         364 AA.
AC   P0A1F1; P15051;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   28-MAR-2018, entry version 90.
DE   RecName: Full=D-alanine--D-alanine ligase A;
DE            EC=6.3.2.4;
DE   AltName: Full=D-Ala-D-Ala ligase A;
DE   AltName: Full=D-alanylalanine synthetase A;
GN   Name=ddlA; OrderedLocusNames=STY0412, t2484;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA   Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA   Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA   Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA   Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA   Whitehead S., Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella
RT   enterica serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA   Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT   and CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000305}.
DR   EMBL; AL513382; CAD08835.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70072.1; -; Genomic_DNA.
DR   RefSeq; NP_454975.1; NC_003198.1.
DR   RefSeq; WP_001096588.1; NZ_PHKG01000009.1.
DR   ProteinModelPortal; P0A1F1; -.
DR   SMR; P0A1F1; -.
DR   STRING; 220341.STY0412; -.
DR   PRIDE; P0A1F1; -.
DR   EnsemblBacteria; AAO70072; AAO70072; t2484.
DR   EnsemblBacteria; CAD08835; CAD08835; CAD08835.
DR   GeneID; 1246892; -.
DR   KEGG; stt:t2484; -.
DR   KEGG; sty:STY0412; -.
DR   PATRIC; fig|220341.7.peg.409; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; RCDFFVI; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-EC.
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-UniPathway.
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; 1.
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; Cell shape; Cell wall biogenesis/degradation;
KW   Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Peptidoglycan synthesis.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    364       D-alanine--D-alanine ligase A.
FT                                /FTId=PRO_0000177867.
FT   DOMAIN      145    348       ATP-grasp.
FT   NP_BIND     175    230       ATP. {ECO:0000250}.
FT   METAL       302    302       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       315    315       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       315    315       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       317    317       Magnesium or manganese 2. {ECO:0000250}.
SQ   SEQUENCE   364 AA;  39357 MW;  00AB43A06746E276 CRC64;
     MAKLRVGIVF GGKSAEHEVS LQSAKNIVDA IDKTRFDVVL LGIDKAGQWH VNDAENYLQN
     ADDPAHIALR PSAISLAQVP GKHQHQLINA QNGQPLPTVD VIFPIVHGTL GEDGSLQGML
     RVANLPFVGS DVLSSAACMD KDVAKRLLRD AGLNIAPFIT LTRTNRHAFS FAEVESRLGL
     PLFVKPANQG SSVGVSKVAN EAQYQQAVAL AFEFDHKVVV EQGIKGREIE CAVLGNDNPQ
     ASTCGEIVLN SEFYAYDTKY IDDNGAQVVV PAQIPSEVND KIRAIAIQAY QTLGCAGMAR
     VDVFLTADNE VVINEINTLP GFTNISMYPK LWQASGLGYT DLISRLIELA LERHTANNAL
     KTTM
//
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