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Database: UniProt/TrEMBL
Entry: A0A0A8GWH9_9PROT
LinkDB: A0A0A8GWH9_9PROT
Original site: A0A0A8GWH9_9PROT 
ID   A0A0A8GWH9_9PROT        Unreviewed;       346 AA.
AC   A0A0A8GWH9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   22-NOV-2017, entry version 21.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|SAAS:SAAS00910572};
DE            EC=6.3.2.4 {ECO:0000256|SAAS:SAAS00910572};
GN   Name=ddlA {ECO:0000313|EMBL:AJC86141.1};
GN   ORFNames=CAQ16704_0670 {ECO:0000313|EMBL:AJC86141.1};
OS   Campylobacter sp. RM16704.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=1500960 {ECO:0000313|EMBL:AJC86141.1, ECO:0000313|Proteomes:UP000031122};
RN   [1] {ECO:0000313|EMBL:AJC86141.1, ECO:0000313|Proteomes:UP000031122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM16704 {ECO:0000313|EMBL:AJC86141.1,
RC   ECO:0000313|Proteomes:UP000031122};
RX   PubMed=25381664; DOI=10.1093/gbe/evu249;
RA   Miller W.G., Yee E., Chapman M.H., Smith T.P., Bono J.L., Huynh S.,
RA   Parker C.T., Vandamme P., Luong K., Korlach J.;
RT   "Comparative Genomics of the Campylobacter lari Group.";
RL   Genome Biol. Evol. 6:3252-3266(2014).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|SAAS:SAAS00910576}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|SAAS:SAAS00910566}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00910571};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00910564};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|SAAS:SAAS00910582}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00644680}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|SAAS:SAAS00910642}.
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DR   EMBL; CP007769; AJC86141.1; -; Genomic_DNA.
DR   RefSeq; WP_039666872.1; NZ_CP007769.1.
DR   EnsemblBacteria; AJC86141; AJC86141; CAQ16704_0670.
DR   KEGG; camr:CAQ16704_0670; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000031122; 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-EC.
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-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 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   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|SAAS:SAAS00644718};
KW   Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS00644792};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031122};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00910562};
KW   Ligase {ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:AJC86141.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00910568};
KW   Manganese {ECO:0000256|SAAS:SAAS00910578};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00910590};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644705};
KW   Peptidoglycan synthesis {ECO:0000256|SAAS:SAAS00644714}.
FT   DOMAIN      133    327       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   346 AA;  39495 MW;  32AC321BFF2F059B CRC64;
     MIYGVIFGAN SYEHEISIVS AVVLKKVLKA QKKFIFCDKN KEFFLINEEK MNAKFFSSGA
     YKKEKVLVLK QGGFFYKTVL GEKKLKIDVA INIVHGKDGE DGKIAALLDF YGVKYIGPRL
     EASVLSFNKI LTKLFAQSVG VKVFDYKTLN LYKKQTKSLK FPCILKPARL GSSIGISIAK
     DENELKYAKD VAFEFDEDII VEEFISNIKE YNLAGCMIDE KIEFSIIEEP KKNQILDFEQ
     KYLGFSESSK VKEADIGESL KQKLRENFTK IYDPLFKGSL IRCDFFVVDN EVYLNEINPN
     PGSLANYLFD DFTQVINQLA KNVELEKQIK INYAFIHNIN GQKGKL
//
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