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Database: UniProt/TrEMBL
Entry: B9L9N9_NAUPA
LinkDB: B9L9N9_NAUPA
Original site: B9L9N9_NAUPA 
ID   B9L9N9_NAUPA            Unreviewed;       344 AA.
AC   B9L9N9;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 59.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|SAAS:SAAS00754435};
DE            EC=6.3.2.4 {ECO:0000256|SAAS:SAAS00754435};
GN   OrderedLocusNames=NAMH_0945 {ECO:0000313|EMBL:ACM93621.1};
OS   Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC   Nautiliaceae; Nautilia.
OX   NCBI_TaxID=598659 {ECO:0000313|EMBL:ACM93621.1, ECO:0000313|Proteomes:UP000000448};
RN   [1] {ECO:0000313|EMBL:ACM93621.1, ECO:0000313|Proteomes:UP000000448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1463 / DSM 18972 / AmH
RC   {ECO:0000313|Proteomes:UP000000448};
RX   PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA   Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y.,
RA   Lee C.K., Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT   "Adaptations to submarine hydrothermal environments exemplified by the
RT   genome of Nautilia profundicola.";
RL   PLoS Genet. 5:E1000362-E1000362(2009).
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; CP001279; ACM93621.1; -; Genomic_DNA.
DR   RefSeq; WP_015902673.1; NC_012115.1.
DR   ProteinModelPortal; B9L9N9; -.
DR   STRING; 598659.NAMH_0945; -.
DR   EnsemblBacteria; ACM93621; ACM93621; NAMH_0945.
DR   KEGG; nam:NAMH_0945; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000102494; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   OrthoDB; POG091H06GK; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000448; 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:UP000000448};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00754427};
KW   Ligase {ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:ACM93621.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000448}.
FT   DOMAIN      136    323       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   344 AA;  39345 MW;  B70E1338D28E2242 CRC64;
     MTFALLFGGN SFEHEISIVS AITLKDKIKK HTLEFIYIDQ NRNMYLVDKQ NMKSKYFASG
     EYKNSQKIEI TKGGFKYTKG LLKKDVFLNY DAVINLIHGK DGEDGKLAGI LEFFNIKSIT
     PNVEASVISY NKVLTKAYAK EIGVNVIDYE IITEPKSSFD FPIIIKPARL GSSIGVSVVK
     TQEEFDYAFD VAREFDDLII AEPFIEGIEE YNLAGCLAGG EFMLSNIEKV EKSDFLDFEK
     KYMDFSRKNV MLSDVDKDLT ERIKKTFKKI YNSTFKNAII RCDFFVKEGS VYLNEINPIP
     GSMANYLFDD FDDVLEKLAK NIESEKEVKI DFEYINKIQM AKGK
//
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