ID   DDLB_XANCP              Reviewed;         318 AA.
AC   Q8PCJ8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-NOV-2008, entry version 44.
DE   RecName: Full=D-alanine--D-alanine ligase B;
DE            EC=6.3.2.4;
DE   AltName: Full=D-alanylalanine synthetase B;
DE   AltName: Full=D-Ala-D-Ala ligase B;
GN   Name=ddlB; OrderedLocusNames=XCC0727;
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; AE012171; AAM40042.1; -; Genomic_DNA.
DR   RefSeq; NP_636118.1; -.
DR   HSSP; P07862; 1IOW.
DR   GeneID; 1001363; -.
DR   GenomeReviews; AE008922_GR; XCC0727.
DR   KEGG; xcc:XCC0727; -.
DR   HOGENOM; Q8PCJ8; -.
DR   BioCyc; XCAM190485:XCC0727-MON; -.
DR   GO; GO:0005618; C:cell wall; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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: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    318       D-alanine--D-alanine ligase B.
FT                                /FTId=PRO_0000177909.
FT   DOMAIN      117    315       ATP-grasp.
FT   NP_BIND     146    201       ATP (By similarity).
FT   METAL       268    268       Magnesium or manganese 1 (By similarity).
FT   METAL       282    282       Magnesium or manganese 1 (By similarity).
FT   METAL       282    282       Magnesium or manganese 2 (By similarity).
FT   METAL       284    284       Magnesium or manganese 2 (By similarity).
SQ   SEQUENCE   318 AA;  33569 MW;  82B6E6AEEB93E1A0 CRC64;
     MSTQIAPARI SDPAAFGRVA VLLGGTSSER EVSLNSGSNV LDALRARGVD AQPVDGIPAL
     AQALVAQRFD RVFNVLHGHN GGGEDGIVQG LMEAFGVPYT GSNVLGSALS MDKIRTKQVW
     LSLGLSTPRY ARLAAGASAQ QIHAAAEQIG LPVIVKPANE GSSVGVSRVF DQAQLDEAVT
     LAARYDGALL MEQLIEGDEL TVAVLGDVAL PSIRIVPKGQ WYDYNAKYIA EDTQYLCPGL
     DGDAEAQIGQ LALDAFRAAG CSGWGRVDVM RDGSTGQLYL LEVNTAPGMT SHSLVPKAAR
     QLGIDFEALV WRVLEQTL
//