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Database: UniProt/TrEMBL
Entry: A0A1C0XAL5_CAMFE
LinkDB: A0A1C0XAL5_CAMFE
Original site: A0A1C0XAL5_CAMFE 
ID   A0A1C0XAL5_CAMFE        Unreviewed;       345 AA.
AC   A0A1C0XAL5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   07-JUN-2017, entry version 7.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|SAAS:SAAS00754435};
DE            EC=6.3.2.4 {ECO:0000256|SAAS:SAAS00754435};
GN   ORFNames=CFT12S05168_01350 {ECO:0000313|EMBL:OCR85990.1};
OS   Campylobacter fetus subsp. testudinum.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=1507806 {ECO:0000313|EMBL:OCR85990.1, ECO:0000313|Proteomes:UP000093179};
RN   [1] {ECO:0000313|EMBL:OCR85990.1, ECO:0000313|Proteomes:UP000093179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT12S05168 {ECO:0000313|EMBL:OCR85990.1,
RC   ECO:0000313|Proteomes:UP000093179};
RX   PubMed=27333878; DOI=10.1093/gbe/evw146;
RA   Gilbert M.J., Miller W.G., Yee E., Zomer A.L.,
RA   van der Graaf-van Bloois L., Fitzgerald C., Forbes K.J., Meric G.,
RA   Sheppard S.K., Wagenaar J.A., Duim B.;
RT   "Comparative Genomics of Campylobacter fetus from Reptiles and Mammals
RT   Reveals Divergent Evolution in Host-Associated Lineages.";
RL   Genome Biol. Evol. 8:2006-2019(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OCR85990.1}.
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DR   EMBL; LELD01000002; OCR85990.1; -; Genomic_DNA.
DR   RefSeq; WP_023384975.1; NZ_LMBG01000030.1.
DR   EnsemblBacteria; OCR85990; OCR85990; CFT12S05168_01350.
DR   GeneID; 28714626; -.
DR   KEGG; cfp:CR44_04080; -.
DR   PATRIC; fig|1507806.10.peg.710; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000093179; Unassembled WGS sequence.
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:UP000093179};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00754427};
KW   Ligase {ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:OCR85990.1};
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}.
FT   DOMAIN      133    325       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   345 AA;  38861 MW;  8755A20CC272B98F CRC64;
     MKFGIVFGGV SFEHEISIVS AIAVKKALKC ELSFIFVDKL GDFYLINSDD MRANFFSSYK
     YKNSKKLHLK KGGFATHGIF GMNDLNVDCY INLIHGRDGE DGKIAGMFEF YNIAFIGPRL
     EASVMSFNKE LTKLLAHKCA VKSLPYEMIK RGDRVKTELP FILKPARLGS SIGVSVVRDI
     SNLDYALDVA FEFDQDILVE PFKEGIREFN LAGFKAENEF IYSFIEEPKK SDFLDFEQKY
     MSFSSSCAKE ASIDDSLKIA IKDAFAKIYN GGNFDGALIR CDFFVLDNEV YLNEINPNPG
     SMANYLFTDF TSSVKKLANS IKPQKNIDID YKFINSITSN KGKLA
//
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