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Database: UniProt
Entry: Q5SHZ3
LinkDB: Q5SHZ3
Original site: Q5SHZ3 
ID   DDL_THET8               Reviewed;         319 AA.
AC   Q5SHZ3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   05-DEC-2018, entry version 96.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE            EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047};
GN   Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=TTHA1587;
OS   Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HB8 / ATCC 27634 / DSM 579;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y.,
RA   Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
CC         phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00047};
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       {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00047}.
DR   EMBL; AP008226; BAD71410.1; -; Genomic_DNA.
DR   RefSeq; WP_011228789.1; NC_006461.1.
DR   RefSeq; YP_144853.1; NC_006461.1.
DR   PDB; 2FB9; X-ray; 1.90 A; A=1-319.
DR   PDB; 2YZG; X-ray; 2.30 A; A/B/C=1-319.
DR   PDB; 2YZM; X-ray; 2.21 A; A/B/C=1-319.
DR   PDB; 2YZN; X-ray; 2.60 A; A/B/C=1-319.
DR   PDB; 2ZDG; X-ray; 2.20 A; A/B/C/D=1-319.
DR   PDB; 2ZDH; X-ray; 1.90 A; A/B/C/D=1-319.
DR   PDB; 2ZDQ; X-ray; 2.30 A; A/B=1-319.
DR   PDBsum; 2FB9; -.
DR   PDBsum; 2YZG; -.
DR   PDBsum; 2YZM; -.
DR   PDBsum; 2YZN; -.
DR   PDBsum; 2ZDG; -.
DR   PDBsum; 2ZDH; -.
DR   PDBsum; 2ZDQ; -.
DR   ProteinModelPortal; Q5SHZ3; -.
DR   SMR; Q5SHZ3; -.
DR   STRING; 300852.TTHA1587; -.
DR   EnsemblBacteria; BAD71410; BAD71410; BAD71410.
DR   GeneID; 3168507; -.
DR   KEGG; ttj:TTHA1587; -.
DR   PATRIC; fig|300852.9.peg.1557; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   PhylomeDB; Q5SHZ3; -.
DR   BioCyc; TTHE300852:G1GKC-1593-MONOMER; -.
DR   BRENDA; 6.3.2.4; 7852.
DR   UniPathway; UPA00219; -.
DR   EvolutionaryTrace; Q5SHZ3; -.
DR   Proteomes; UP000000532; 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-UniRule.
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-UniRule.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN         1    319       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341188.
FT   DOMAIN      120    315       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     147    198       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       270    270       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       282    282       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       282    282       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       284    284       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   STRAND        3      8       {ECO:0000244|PDB:2ZDH}.
FT   HELIX        14     27       {ECO:0000244|PDB:2ZDH}.
FT   STRAND       32     37       {ECO:0000244|PDB:2ZDH}.
FT   HELIX        46     55       {ECO:0000244|PDB:2ZDH}.
FT   HELIX        71     73       {ECO:0000244|PDB:2ZDH}.
FT   STRAND       75     79       {ECO:0000244|PDB:2ZDH}.
FT   TURN         84     87       {ECO:0000244|PDB:2ZDH}.
FT   HELIX        90     98       {ECO:0000244|PDB:2ZDH}.
FT   STRAND      102    104       {ECO:0000244|PDB:2ZDH}.
FT   HELIX       107    114       {ECO:0000244|PDB:2ZDH}.
FT   HELIX       118    125       {ECO:0000244|PDB:2ZDH}.
FT   STRAND      133    137       {ECO:0000244|PDB:2ZDH}.
FT   STRAND      150    156       {ECO:0000244|PDB:2ZDH}.
FT   TURN        159    162       {ECO:0000244|PDB:2ZDH}.
FT   STRAND      164    168       {ECO:0000244|PDB:2ZDH}.
FT   HELIX       169    171       {ECO:0000244|PDB:2ZDH}.
FT   HELIX       172    180       {ECO:0000244|PDB:2ZDH}.
FT   STRAND      184    190       {ECO:0000244|PDB:2ZDH}.
FT   STRAND      196    207       {ECO:0000244|PDB:2ZDH}.
FT   STRAND      209    217       {ECO:0000244|PDB:2ZDH}.
FT   STRAND      219    222       {ECO:0000244|PDB:2ZDH}.
FT   HELIX       225    229       {ECO:0000244|PDB:2ZDH}.
FT   TURN        231    233       {ECO:0000244|PDB:2ZDH}.
FT   STRAND      234    239       {ECO:0000244|PDB:2ZDH}.
FT   HELIX       244    261       {ECO:0000244|PDB:2ZDH}.
FT   STRAND      265    274       {ECO:0000244|PDB:2ZDH}.
FT   STRAND      277    286       {ECO:0000244|PDB:2ZDH}.
FT   HELIX       294    301       {ECO:0000244|PDB:2ZDH}.
FT   HELIX       306    317       {ECO:0000244|PDB:2ZDH}.
SQ   SEQUENCE   319 AA;  34666 MW;  85E6F0AA367A13AF CRC64;
     MRVLLIAGGV SPEHEVSLLS AEGVLRHIPF PTDLAVIAQD GRWLLGEKAL TALEAKAAPE
     GEHPFPPPLS WERYDVVFPL LHGRFGEDGT VQGFLELLGK PYVGAGVAAS ALCMDKDLSK
     RVLAQAGVPV VPWVAVRKGE PPVVPFDPPF FVKPANTGSS VGISRVERFQ DLEAALALAF
     RYDEKAVVEK ALSPVRELEV GVLGNVFGEA SPVGEVRYEA PFYDYETKYT PGRAELLIPA
     PLDPGTQETV QELALKAYKV LGVRGMARVD FFLAEGELYL NELNTIPGFT PTSMYPRLFE
     AGGVAYPELL RRLVELALT
//
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