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Database: UniProt/TrEMBL
Entry: D4M2C0_9FIRM
LinkDB: D4M2C0_9FIRM
Original site: D4M2C0_9FIRM 
ID   D4M2C0_9FIRM            Unreviewed;       350 AA.
AC   D4M2C0;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-SEP-2017, entry version 51.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754435};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754435};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
GN   Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   ORFNames=RTO_06490 {ECO:0000313|EMBL:CBL25382.1};
OS   Ruminococcus torques L2-14.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Blautia.
OX   NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL25382.1, ECO:0000313|Proteomes:UP000008956};
RN   [1] {ECO:0000313|EMBL:CBL25382.1, ECO:0000313|Proteomes:UP000008956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-14 {ECO:0000313|EMBL:CBL25382.1,
RC   ECO:0000313|Proteomes:UP000008956};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Ruminococcus torques L2-14.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL25382.1, ECO:0000313|Proteomes:UP000008956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-14 {ECO:0000313|EMBL:CBL25382.1,
RC   ECO:0000313|Proteomes:UP000008956};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00754456}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00754451}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR039102-3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00754454};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00644680}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00644812}.
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DR   EMBL; FP929055; CBL25382.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4M2C0; -.
DR   STRING; 657313.RTO_06490; -.
DR   EnsemblBacteria; CBL25382; CBL25382; RTO_06490.
DR   KEGG; rto:RTO_06490; -.
DR   PATRIC; fig|657313.3.peg.327; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008956; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644673};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644718};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644792};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008956};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00754427};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:CBL25382.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00754439};
KW   Manganese {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00754447};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00754442};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644705};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008956}.
FT   DOMAIN      147    343       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   METAL       297    297       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       310    310       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       310    310       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       312    312       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ   SEQUENCE   350 AA;  37954 MW;  BDB154BA1400550A CRC64;
     MKIIVLAGGL STERDVSLSS AAGICRTLVE KGHDAFLLDV FMGLENAPEN LEDVFTLPDH
     GLEIVKNIST EEPDLEAVKA SRPDQSDCFF GPNVIELCRL ADITFLGLHG GEGENGKLQA
     SFDLLGIKYT GPDSLGCAVA MHKGVAKQIF LESGVDTPGG GTIYKNSEDQ SYQSLGLTLP
     VVVKPCSGGS SIGVYIVNTD EEYAEALKKS FRYEDELVVE PYIKGREFAC GIIDGTALPP
     IEIIPKTGFF DYANKYQDGA TSEVCPADIP EEVAERMKEL TVKAFNALKL NVYSRADFLL
     DAEGNLFCLE MNTLPGMTSA SLLPKEAKVY GIEYGDLCEL IIKKSMEARY
//
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