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Database: UniProt/TrEMBL
Entry: A7GYC3_CAMC5
LinkDB: A7GYC3_CAMC5
Original site: A7GYC3_CAMC5 
ID   A7GYC3_CAMC5            Unreviewed;       347 AA.
AC   A7GYC3;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   07-JUN-2017, entry version 80.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|SAAS:SAAS00754435};
DE            EC=6.3.2.4 {ECO:0000256|SAAS:SAAS00754435};
GN   Name=ddlA {ECO:0000313|EMBL:EAT99804.1};
GN   ORFNames=CCV52592_1152 {ECO:0000313|EMBL:EAT99804.1};
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105 {ECO:0000313|EMBL:EAT99804.1, ECO:0000313|Proteomes:UP000006380};
RN   [1] {ECO:0000313|Proteomes:UP000006380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|SAAS:SAAS00754456}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {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|SAAS:SAAS00754475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00644680}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|SAAS:SAAS00644812}.
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DR   EMBL; CP000767; EAT99804.1; -; Genomic_DNA.
DR   RefSeq; WP_011992262.1; NC_009715.2.
DR   ProteinModelPortal; A7GYC3; -.
DR   STRING; 360105.CCV52592_1152; -.
DR   EnsemblBacteria; EAT99804; EAT99804; CCV52592_1152.
DR   KEGG; ccv:CCV52592_1152; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000102494; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000006380; 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.
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.
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:UP000006380};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00754427};
KW   Ligase {ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:EAT99804.1};
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|SAAS:SAAS00644714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006380}.
FT   DOMAIN      133    324       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   347 AA;  39781 MW;  F26A795969764B80 CRC64;
     MKLGVVFGAK SFEHEISIVS AIVLKNVLKQ ELSFIFCDKE RKFYLIEPTD MRANFFSSGK
     YKKCKKLFLM ACGFYTHSLF GVKRLEVDVY INLIHGMDGE DGKFASLFDF YGISYIGPRL
     EASVMSYNKE LTKFLAQKVG VKTLDYEMIT YEELPKFALP IILKPARLGS SIGVSVVKDE
     SEFEYARDVA FEFDKEVLVE PFIEGVKEYN LAGCMIDGKM RFSIVEEPKK KEFLDYEQKY
     MSFSNESKAQ EARIDEELRD RLKENFVKIY GFGFEGAIIR CDFFVIEGEV YLNEINPNPG
     SLANYLFEDF EAMLNALAAS RLPKERKINI DYKFINSITS AKGSGKI
//
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