ID   DDLA_XANCP              Reviewed;         373 AA.
AC   Q8PDW3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 45.
DE   RecName: Full=D-alanine--D-alanine ligase A;
DE            EC=6.3.2.4;
DE   AltName: Full=D-alanylalanine synthetase A;
DE   AltName: Full=D-Ala-D-Ala ligase A;
GN   Name=ddlA; Synonyms=ddlB; OrderedLocusNames=XCC0222;
OS   Xanthomonas campestris pv. campestris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
RX   MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
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; AE012118; AAM39541.1; -; Genomic_DNA.
DR   RefSeq; NP_635617.2; -.
DR   HSSP; P25051; 1E4E.
DR   GeneID; 999929; -.
DR   GenomeReviews; AE008922_GR; XCC0222.
DR   KEGG; xcc:XCC0222; -.
DR   HOGENOM; Q8PDW3; -.
DR   OMA; Q8PDW3; GREIECG.
DR   BioCyc; XCAM190485:XCC0222-MON; -.
DR   BRENDA; 6.3.2.4; 281360.
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:UniProtKB-KW.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00047; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
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; IPR013817; Pre-ATP_grasp.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 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    373       D-alanine--D-alanine ligase A.
FT                                /FTId=PRO_0000177908.
FT   DOMAIN      150    353       ATP-grasp.
FT   NP_BIND     180    235       ATP (By similarity).
FT   METAL       307    307       Magnesium or manganese 1 (By similarity).
FT   METAL       320    320       Magnesium or manganese 1 (By similarity).
FT   METAL       320    320       Magnesium or manganese 2 (By similarity).
FT   METAL       322    322       Magnesium or manganese 2 (By similarity).
SQ   SEQUENCE   373 AA;  40110 MW;  01E285702AF9D15F CRC64;
     MTGAGMRRIR VGLIFGGKSA EHEVSLQSAR NILQALDPQR FEPVLIGIDK QGQWHLSAQE
     SFLLDADDPS RIALRHSGRG LAVLPGAASA QLRAVDAEQA LAQIDVVFPI VHGTLGEDGS
     LQGLLRMANL PFVGSGVLGS AVAMDKDMAK RVLRDAGLEV APFACFTRHT AAQADVQTLI
     AQFGLPLFVK PANQGSSVGV SQVRSAEEFS AALELALRYD HKVLVEAAIA GREIECAVLG
     NATPQASVCG EVVVHDAFYS YQTKYIRDDG AATVIPADID AHTQHRIQQC ALQAYQALDC
     AGMARVDVFL CADGRIVINE VNTLPGFTRI SMYPKLWEAS GLDYRSLVTR LIELALERHA
     DDGRLYSSVV THA
//