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Database: UniProt
Entry: Q8X9Y6
LinkDB: Q8X9Y6
Original site: Q8X9Y6 
ID   DDLB_ECO57              Reviewed;         306 AA.
AC   Q8X9Y6;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   29-OCT-2014, entry version 93.
DE   RecName: Full=D-alanine--D-alanine ligase B;
DE            EC=6.3.2.4;
DE   AltName: Full=D-Ala-D-Ala ligase B;
DE   AltName: Full=D-alanylalanine synthetase B;
GN   Name=ddlB; OrderedLocusNames=Z0102, ECs0096;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine.
CC   -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000305}.
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DR   EMBL; AE005174; AAG54396.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33519.1; -; Genomic_DNA.
DR   PIR; H85491; H85491.
DR   PIR; H90640; H90640.
DR   RefSeq; NP_285788.1; NC_002655.2.
DR   RefSeq; NP_308123.1; NC_002695.1.
DR   ProteinModelPortal; Q8X9Y6; -.
DR   SMR; Q8X9Y6; 1-306.
DR   STRING; 155864.Z0102; -.
DR   EnsemblBacteria; AAG54396; AAG54396; Z0102.
DR   EnsemblBacteria; BAB33519; BAB33519; BAB33519.
DR   GeneID; 913558; -.
DR   GeneID; 956778; -.
DR   KEGG; ece:Z0102; -.
DR   KEGG; ecs:ECs0096; -.
DR   PATRIC; 18349134; VBIEscCol44059_0097.
DR   eggNOG; COG1181; -.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; EDPARES; -.
DR   OrthoDB; EOG6ND0KB; -.
DR   BioCyc; ECOL386585:GJFA-94-MONOMER; -.
DR   BioCyc; ECOO157:DDLB-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-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; 2.
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    306       D-alanine--D-alanine ligase B.
FT                                /FTId=PRO_0000177820.
FT   DOMAIN      101    303       ATP-grasp.
FT   NP_BIND     134    189       ATP. {ECO:0000250}.
FT   ACT_SITE     15     15       {ECO:0000250}.
FT   ACT_SITE    150    150       {ECO:0000250}.
FT   ACT_SITE    281    281       {ECO:0000250}.
FT   METAL       257    257       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       270    270       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       270    270       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       272    272       Magnesium or manganese 2. {ECO:0000250}.
SQ   SEQUENCE   306 AA;  32854 MW;  3302284E030DD647 CRC64;
     MTDKIAVLLG GTSAEREVSL NSGAAVLAGL REGGIDAYPV DPKEVDVTQL KSMGFQKVFI
     ALHGRGGEDG TLQGMLELMG LPYTGSGVMA SALSMDKLRS KLLWQGAGLP VAPWVALTRV
     EFEKGLSDKQ LAEISALGLP VIVKPSREGS SVGMSKVVAE NALQDALRLA FQHDEEVLIE
     KWLSGPEFTV AILGEEILPS VRIQPSGTFY DYEAKYLSDE TQYFCPAGLE ASQEANLQAL
     VLKAWTTLGC KGWGRIDVML DSDGQFYLLE ANTSPGMTSH SLVPMAARQA GMSFSQLVVR
     ILELAD
//
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