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Database: UniProt/TrEMBL
Entry: I7H4L6_9HELI
LinkDB: I7H4L6_9HELI
Original site: I7H4L6_9HELI 
ID   I7H4L6_9HELI            Unreviewed;       345 AA.
AC   I7H4L6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   05-JUL-2017, entry version 38.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|SAAS:SAAS00754435};
DE            EC=6.3.2.4 {ECO:0000256|SAAS:SAAS00754435};
GN   Name=ddl {ECO:0000313|EMBL:BAM31930.1};
GN   ORFNames=HCBAA847_0692 {ECO:0000313|EMBL:BAM31930.1};
OS   Helicobacter cinaedi CCUG 18818 = ATCC BAA-847.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537971 {ECO:0000313|EMBL:BAM31930.1, ECO:0000313|Proteomes:UP000006036};
RN   [1] {ECO:0000313|EMBL:BAM31930.1, ECO:0000313|Proteomes:UP000006036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM31930.1,
RC   ECO:0000313|Proteomes:UP000006036};
RX   PubMed=23012276; DOI=10.1128/JB.01347-12;
RA   Miyoshi-Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RT   "Complete Genome Sequence of Helicobacter cinaedi Type Strain ATCC
RT   BAA-847.";
RL   J. Bacteriol. 194:5692-5692(2012).
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; AP012492; BAM31930.1; -; Genomic_DNA.
DR   RefSeq; WP_002956343.1; NZ_DS990392.1.
DR   STRING; 537971.HCCG_01032; -.
DR   EnsemblBacteria; BAM31930; BAM31930; HCBAA847_0692.
DR   KEGG; hcb:HCBAA847_0692; -.
DR   PATRIC; fig|1206745.3.peg.719; -.
DR   KO; K01921; -.
DR   OrthoDB; POG091H06GK; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000006036; Chromosome 1.
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.
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:UP000006036};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00754427};
KW   Ligase {ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:BAM31930.1};
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:UP000006036}.
FT   DOMAIN      134    332       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   345 AA;  39142 MW;  C4EB4CDE9E0E858F CRC64;
     MKFDVIFGGV SFEHEISIVS AVALKKVLGE RISNFIFLDS LHRFYLIPAT LMKSKTFSSG
     EYKKCTEIFL QRSSFVKKSL FGFKAIIPNT LISLIHGADG EDGSMSALLD FYHIPFIGPR
     IESSVMSFNK ALTKIYAQSR GVKVLDHEIL TRNSPNPTLP YPLILKPSRL GSSIGVSVVN
     KEDELEYAKD LAFEYDDSIV VECFKSGVKE YNLAGCKIGD EFRFSIVEEP SKKEMLDFEN
     KYLDFSRTAQ VLKADISQEL EKQIQQNFAK LYENAFEGAL IRCDFFVIDN EVYLNEINPI
     PGSMANYLFE DFACVLESLA HNLPKKHSIK VSYKYIERIH HAKGK
//
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