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Entry: A0A0M1UL49_9PROT
LinkDB: A0A0M1UL49_9PROT
Original site: A0A0M1UL49_9PROT 
ID   A0A0M1UL49_9PROT        Unreviewed;       347 AA.
AC   A0A0M1UL49;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   25-OCT-2017, entry version 15.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|SAAS:SAAS00910572};
DE            EC=6.3.2.4 {ECO:0000256|SAAS:SAAS00910572};
GN   ORFNames=ABED_0693 {ECO:0000313|EMBL:BAK70410.1};
OS   Arcobacter butzleri ED-1.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Arcobacter.
OX   NCBI_TaxID=944546 {ECO:0000313|EMBL:BAK70410.1, ECO:0000313|Proteomes:UP000009194};
RN   [1] {ECO:0000313|EMBL:BAK70410.1, ECO:0000313|Proteomes:UP000009194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED-1 {ECO:0000313|Proteomes:UP000009194};
RX   PubMed=22038970; DOI=10.1128/JB.06084-11;
RA   Toh H., Sharma V.K., Oshima K., Kondo S., Hattori M., Ward F.B.,
RA   Free A., Taylor T.D.;
RT   "Complete Genome Sequences of Arcobacter butzleri ED-1 and Arcobacter
RT   sp. Strain L, Both Isolated from a Microbial Fuel Cell.";
RL   J. Bacteriol. 193:6411-6412(2011).
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; AP012047; BAK70410.1; -; Genomic_DNA.
DR   RefSeq; WP_014468431.1; NC_017187.1.
DR   EnsemblBacteria; BAK70410; BAK70410; ABED_0693.
DR   KEGG; abt:ABED_0693; -.
DR   PATRIC; fig|944546.4.peg.698; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000009194; 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.
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:UP000009194};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00910562};
KW   Ligase {ECO:0000256|SAAS:SAAS00644741};
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}.
FT   DOMAIN      136    330       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   347 AA;  39489 MW;  E884B09E79645E94 CRC64;
     MKVAIVFGGI SFEHEISIVS SIALKDVLKK DEIIYLFLDS SRQMYHIPTN IIKSKLFSSG
     EYKKFDKVYF QRGGFYKKGG VFSKDKNIDF DVVLNLSHGG DGEDGILSSV LDFYSIPFIA
     PRTEACVVSS NKFLTKGYAK SVNVNTLDYK YFTKDDKIKV DSFPVILKPV KLGSSIGVAI
     VKSQEELQYA LDVAFEFDDA IIIEPFISGV KEYNLAGTKV NGEFKFSIIE EPQKAEFLDF
     DKKYLDFSRT SKAKEVNLGE KLNNEIKESF KRLYNTLFEG SIIRCDFFVI NDEIYLNEIN
     SIPGSMANYL FEDFQSLFNQ VAKNLPRKKH IPITYEYVNK IHSAKGK
//
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