GenomeNet

Database: UniProt/TrEMBL
Entry: W6EEV5_SULMU
LinkDB: W6EEV5_SULMU
Original site: W6EEV5_SULMU 
ID   W6EEV5_SULMU            Unreviewed;       344 AA.
AC   W6EEV5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   22-NOV-2017, entry version 30.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
GN   Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047,
GN   ECO:0000313|EMBL:AHJ12738.1};
GN   ORFNames=SMUL_1478 {ECO:0000313|EMBL:AHJ12738.1};
OS   Sulfurospirillum multivorans DSM 12446.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Sulfurospirillum.
OX   NCBI_TaxID=1150621 {ECO:0000313|EMBL:AHJ12738.1, ECO:0000313|Proteomes:UP000019322};
RN   [1] {ECO:0000313|EMBL:AHJ12738.1, ECO:0000313|Proteomes:UP000019322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12446 {ECO:0000313|EMBL:AHJ12738.1,
RC   ECO:0000313|Proteomes:UP000019322};
RX   PubMed=25186071; DOI=10.1111/1462-2920.12589;
RA   Goris T., Schubert T., Gadkari J., Wubet T., Tarkka M., Buscot F.,
RA   Adrian L., Diekert G.;
RT   "Insights into organohalide respiration and the versatile catabolism
RT   of Sulfurospirillum multivorans gained from comparative genomics and
RT   physiological studies.";
RL   Environ. Microbiol. 16:3562-3580(2014).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00910576}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       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|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910582}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00644680}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910642}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP007201; AHJ12738.1; -; Genomic_DNA.
DR   RefSeq; WP_025344613.1; NZ_CP007201.1.
DR   EnsemblBacteria; AHJ12738; AHJ12738; SMUL_1478.
DR   KEGG; smul:SMUL_1478; -.
DR   PATRIC; fig|1150621.9.peg.1482; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000019322; 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-UniRule.
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-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_00047; Dala_Dala_lig; 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|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644718};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644792};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019322};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00910562};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:AHJ12738.1};
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|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644714}.
FT   DOMAIN      133    327       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   344 AA;  39110 MW;  AAF5589199D702C6 CRC64;
     MTVAVLFGAQ SFEHEISVVS AIALKKVLKC DIVYIFCDYE RNFYLIPTDK ITSKRFSSGE
     YKKDKTLFLK QGGFYAKKML GEEKVAFDVM INLVHGRDGE DGKLSSMLDF FGVPYIGPRT
     EGSCISYNKL FTKLYAGEVG VNVLDYQALR KGSDELIRIP YPFIVKPLRL GSSIGIGIVK
     EKKELEYALD VAFEFDDTVL IEPFISGVKE YNLAGCKTDT FQFSIIEEPQ KEEFLDFDKK
     YLDFSRTKRV NEATLDAQEE AGIKEAFERL YDPLFLGALI RCDFFVVEGK VYLNEINPIP
     GSMANYLFDD FDSVIKALSN YLPKDITMSK EYRYINSIQA AKGK
//
DBGET integrated database retrieval system