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Database: UniProt/TrEMBL
Entry: A0A1S6U6Z8_9PROT
LinkDB: A0A1S6U6Z8_9PROT
Original site: A0A1S6U6Z8_9PROT 
ID   A0A1S6U6Z8_9PROT        Unreviewed;       345 AA.
AC   A0A1S6U6Z8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   20-DEC-2017, entry version 8.
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:AQW87452.1};
GN   ORFNames=CPIN18021_0632 {ECO:0000313|EMBL:AQW87452.1};
OS   Campylobacter pinnipediorum subsp. caledonicus.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=1874362 {ECO:0000313|EMBL:AQW87452.1, ECO:0000313|Proteomes:UP000190868};
RN   [1] {ECO:0000313|Proteomes:UP000190868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM18021 {ECO:0000313|Proteomes:UP000190868};
RA   Miller W.G., Yee E., Chapman M.H., Huynh S., Bono J.L., On S.L.W.,
RA   StLeger J., Foster G., Parker C.T.;
RT   "Comparative genomics of the Campylobacter concisus group.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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; CP017258; AQW87452.1; -; Genomic_DNA.
DR   KEGG; cpin:CPIN18020_0627; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000190868; 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:UP000190868};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00910562};
KW   Ligase {ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:AQW87452.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190868}.
FT   DOMAIN      133    326       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   345 AA;  39323 MW;  9FE099C38D1A9AF2 CRC64;
     MKLGIVFGAK SFEHEISVVS AIVLKNVLNE ECVFVFCDSL REFYLIESKN MKANFFSKGL
     YKKSKKLTLK QGGFYTTSMF GESKINADIF INLIHGMDGE DGKIASLFDF FGVDYIGPRL
     EASVLSFNKE LTKLFAKKVG VKTLDYEVIR REDNPKTSYP FILKPLRLGS SIGVSVVKTQ
     DEFDYAKDIA FEFDSDVLVE PFVENVKEYN LAGCIIDDEF KFSIIEEPKK SDFLDFEQKY
     LSFSNEQKVK SADISKELED GLKNAFMKIY KNTFEGALIR CDFFVIDNEI YLNEINPNPG
     SLAHYLFDDF KNIIISLSNS LPDKQNINID YKFLSSIISS KGNKI
//
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