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Database: UniProt/TrEMBL
Entry: G2IM17_9SPHN
LinkDB: G2IM17_9SPHN
Original site: G2IM17_9SPHN 
ID   G2IM17_9SPHN            Unreviewed;       323 AA.
AC   G2IM17;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   22-NOV-2017, entry version 51.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047};
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=ddlA {ECO:0000313|EMBL:BAK65272.1};
GN   Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   ORFNames=SLG_05970 {ECO:0000313|EMBL:BAK65272.1};
OS   Sphingobium sp. SYK-6.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=627192 {ECO:0000313|EMBL:BAK65272.1, ECO:0000313|Proteomes:UP000001275};
RN   [1] {ECO:0000313|EMBL:BAK65272.1, ECO:0000313|Proteomes:UP000001275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SYK-6 {ECO:0000313|EMBL:BAK65272.1,
RC   ECO:0000313|Proteomes:UP000001275};
RX   PubMed=22207743; DOI=10.1128/JB.06254-11;
RA   Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA   Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S.,
RA   Katano Y., Narita-Yamada S., Nakazawa H., Hara H., Katayama Y.,
RA   Fukuda M., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader
RT   of lignin-derived biaryls and monoaryls.";
RL   J. Bacteriol. 194:534-535(2012).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047}.
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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047}.
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:SAAS00910642}.
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DR   EMBL; AP012222; BAK65272.1; -; Genomic_DNA.
DR   RefSeq; WP_014074923.1; NC_015976.1.
DR   STRING; 627192.SLG_05970; -.
DR   EnsemblBacteria; BAK65272; BAK65272; SLG_05970.
DR   KEGG; ssy:SLG_05970; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   KO; K01921; -.
DR   OrthoDB; POG091H00GT; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001275; 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   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
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; 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 {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:UP000001275};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:BAK65272.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR039102-3};
KW   Manganese {ECO:0000256|PIRSR:PIRSR039102-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039102-3};
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:UP000001275}.
FT   DOMAIN      109    309       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   METAL       260    260       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       276    276       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       276    276       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       278    278       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ   SEQUENCE   323 AA;  34336 MW;  7510EB15034F0E09 CRC64;
     MSGPWKVAVL MGGWSAEREV SLSSGAGIVK ALEERGHSAI PIDLGASPAE GRDLPAKLIA
     ADPDIVFNAL HGVPGEDGTV QGLMDIMGYR YTHSGLATSV IAIDKQLTKQ HLVPHGIPMP
     GGHIVASEDL FAADPLPRPY VVKPVNEGSS VGVAIVTAEG NYGNPIGRDV KGPWQEFDEL
     LAEPFIRGRE LTVAVLGDRA LAVTELKPRS GFYDYDAKYT DGMTEHVCPA DVPVDIAQAM
     MDIALRAHRL LGCKGTSRSD FRWDDEQGVE GLFLLEVNTQ PGMTPLSLVP EQARHLGMSY
     GALVEAIIAD ALAEGTPAKG AKE
//
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