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Database: UniProt/TrEMBL
Entry: G2HUN7_9PROT
LinkDB: G2HUN7_9PROT
Original site: G2HUN7_9PROT 
ID   G2HUN7_9PROT            Unreviewed;       346 AA.
AC   G2HUN7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   07-JUN-2017, entry version 41.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|SAAS:SAAS00754435};
DE            EC=6.3.2.4 {ECO:0000256|SAAS:SAAS00754435};
GN   ORFNames=ABLL_0965 {ECO:0000313|EMBL:BAK72840.1};
OS   Arcobacter sp. L.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Arcobacter.
OX   NCBI_TaxID=944547 {ECO:0000313|EMBL:BAK72840.1, ECO:0000313|Proteomes:UP000001290};
RN   [1] {ECO:0000313|EMBL:BAK72840.1, ECO:0000313|Proteomes:UP000001290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L {ECO:0000313|Proteomes:UP000001290};
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: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; AP012048; BAK72840.1; -; Genomic_DNA.
DR   RefSeq; WP_014473677.1; NC_017192.1.
DR   STRING; 944547.ABLL_0965; -.
DR   EnsemblBacteria; BAK72840; BAK72840; ABLL_0965.
DR   KEGG; arc:ABLL_0965; -.
DR   PATRIC; fig|944547.4.peg.975; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   KO; K01921; -.
DR   OrthoDB; POG091H06GK; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001290; 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:UP000001290};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00754427};
KW   Ligase {ECO:0000256|SAAS:SAAS00644741};
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      135    325       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   346 AA;  39228 MW;  676E407BD6EE2B56 CRC64;
     MKVAIVFGGV SFEHEISIVS AIAMKDVLKE ELIYLFLDPS RNMYHIPTNI IKSKLFSSGD
     YKKFEKVYFQ KGGFYKKGGF LSKDKEVDFD VVLNLSHGGD GEDGILSSVL DFYDIPFIAP
     RTEACVISSN KFLTKGYASS VEVNTLDYKY YTKGEIVCVD SFPVILKPVK LGSSIGVSIV
     KSQEELEYAL DVAYEFDNAV IIEPFISGVK EYNLAGTKVN GEFRFSIIEE PQKAEFLDFD
     KKYLDFSRTS KAKEVNLGEK LNTQIKESFK RLYNTLFEGS IIRCDFFVVD DKVYLNEINS
     IPGSMANYLF EDFANLFEEV ANNLPQKKHI PITYEYVNKI HASKGK
//
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