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Database: UniProt/TrEMBL
Entry: A0A1P8KKS1_9PROT
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Original site: A0A1P8KKS1_9PROT 
ID   A0A1P8KKS1_9PROT        Unreviewed;       346 AA.
AC   A0A1P8KKS1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   22-NOV-2017, entry version 7.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|SAAS:SAAS00910572};
DE            EC=6.3.2.4 {ECO:0000256|SAAS:SAAS00910572};
GN   ORFNames=LPB137_04485 {ECO:0000313|EMBL:APW65149.1};
OS   Arcobacter sp. LPB0137.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Arcobacter.
OX   NCBI_TaxID=1850254 {ECO:0000313|EMBL:APW65149.1, ECO:0000313|Proteomes:UP000186074};
RN   [1] {ECO:0000313|EMBL:APW65149.1, ECO:0000313|Proteomes:UP000186074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0137 {ECO:0000313|EMBL:APW65149.1,
RC   ECO:0000313|Proteomes:UP000186074};
RA   Lee G.-W., Yi H.;
RT   "Genome sequencing of Arcobacter sp. LPB0137.";
RL   Submitted (JAN-2017) 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; CP019070; APW65149.1; -; Genomic_DNA.
DR   RefSeq; WP_076084929.1; NZ_CP019070.1.
DR   KEGG; alp:LPB137_04485; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000186074; 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:UP000186074};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00910562};
KW   Ligase {ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:APW65149.1};
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:UP000186074}.
FT   DOMAIN      135    329       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   346 AA;  38833 MW;  EF9038C6B8585C4A CRC64;
     MKIAVVFGGV SFEHEISIVS SIAMKDVLSD ELVYIFLDEN RDFYHIPTNT IKSKLFSSGE
     YKKCDKVTIS KNGFFKKAGL LGKDKPIDFD VVLNLSHGGD GEDGILSSVL EFFNIPFIAP
     RTEACVVSSN KFLTKGYASS VDVKTIDYKY YTKGDSVTVD TFPVIVKPVR LGSSIGVAIV
     KTQEELDYSL DVAYEFDNAI IIEPFISGVK EYNLAGTKVN GEFKFSIIEE PQKTEFLDFD
     KKYLDFSRTS KAVEVDLGEE LNAKVKDAFE KIYNNLFEGS IIRCDFFIVD NEVYLNEINS
     IPGSMANYLF SNFDTLFKSV ATSLPRKKHI PVTYEYVNKI HASKGK
//
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