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Database: UniProt/TrEMBL
Entry: A0A0A8H4K9_CAMLA
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ID   A0A0A8H4K9_CAMLA        Unreviewed;       346 AA.
AC   A0A0A8H4K9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-SEP-2017, entry version 21.
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=ddlA {ECO:0000313|EMBL:AJC89058.1};
GN   Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   ORFNames=CONCH_0643 {ECO:0000313|EMBL:AJC89058.1};
OS   Campylobacter lari subsp. concheus LMG 11760.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=1031536 {ECO:0000313|EMBL:AJC89058.1, ECO:0000313|Proteomes:UP000031115};
RN   [1] {ECO:0000313|EMBL:AJC89058.1, ECO:0000313|Proteomes:UP000031115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG11760 {ECO:0000313|Proteomes:UP000031115};
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|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|SAAS:SAAS00754472};
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; CP007771; AJC89058.1; -; Genomic_DNA.
DR   RefSeq; WP_039668273.1; NZ_CP007771.1.
DR   EnsemblBacteria; AJC89058; AJC89058; CONCH_0643.
DR   KEGG; cll:CONCH_0643; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000031115; 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   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:UP000031115};
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:AJC89058.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00754439};
KW   Manganese {ECO:0000256|SAAS:SAAS00754447};
KW   Metal-binding {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}.
FT   DOMAIN      133    327       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   346 AA;  39240 MW;  5F6D42A222A6F71E CRC64;
     MIYGVIFGAN SYEHEISIVS AVVLKKVLKV QKKFIFCDKN KEFFLIDEEK MNAKTFSSGA
     YKKEKALVLK QGGFFIKTML GEKKLDIDVA VNIVHGKDGE DGKIAALLDF YGIKYIGPRI
     EASVLSFNKV LTKLYAQSVG VKTLDYKVLN LHKEQNVSLD FPCILKPARL GSSIGISIVK
     DESELKYAKD VAFEFDEEVV VEKFVSNIKE YNLAGCMIGE KMEFSIIEEP RKNEILDFEQ
     KYLGFSESSK VSEANISEEL KQKLRDNFTR IYNPLFKGAL IRCDFFVIGD EVYLNEINPN
     PGSLANYLFE DFTNTVDNLA KNIELEKQIK IDYAFIHSIN GQKGKL
//
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