ID   DDLB_CLOTE              Reviewed;         358 AA.
AC   Q898Z5;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, 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=CTC_00291;
OS   Clostridium tetani.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   MEDLINE=22457253; PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of
RT   tetanus disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO34934.1; -; Genomic_DNA.
DR   RefSeq; NP_780997.1; -.
DR   HSSP; P71454; 1EHI.
DR   GeneID; 1059868; -.
DR   GenomeReviews; AE015927_GR; CTC_00291.
DR   KEGG; ctc:CTC00291; -.
DR   NMPDR; fig|212717.1.peg.219; -.
DR   HOGENOM; Q898Z5; -.
DR   BioCyc; CTET212717:CTC_00291-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    358       D-alanine--D-alanine ligase B.
FT                                /FTId=PRO_0000177810.
FT   DOMAIN      147    352       ATP-grasp.
FT   NP_BIND     179    234       ATP (By similarity).
FT   METAL       305    305       Magnesium or manganese 1 (By similarity).
FT   METAL       319    319       Magnesium or manganese 1 (By similarity).
FT   METAL       319    319       Magnesium or manganese 2 (By similarity).
FT   METAL       321    321       Magnesium or manganese 2 (By similarity).
SQ   SEQUENCE   358 AA;  40536 MW;  36E6E9FA2AF9B8F9 CRC64;
     MLLAQQLNLY ILKGEIIMKK IKIAIVFGGQ STEHEVSRNS VTSILKNINR DKYEICPIGI
     TKEGKWFQYT GDINNIKNGQ WEKDNKNKLE NGYNVLFNKE VELVFPVLHG LYGEDGTIQG
     LCKLVGLPCV GPGVLSSALC MDKIYTKYVL ENFKFKQANY VVVNKFEYEK NKEEIIKEVE
     KLQYDVFIKP ANSGSSVGIT KAHNKEELLK GLEEAFIHDK NVLVEEAINA REIEVAVLGN
     DDPKAAVPGE IIPAKEFYDY EAKYQNENSE LLIPANIDNI KQEEIKELAI KIYKLLGCSG
     LARVDFLMDK ESNEVYFNEV NTLPGFTKIS MYPKLWEASG KSYSALIDEL IELAINNK
//