SWISSPROT: D3UY82_XENBS

ID   D3UY82_XENBS            Unreviewed;       365 AA.
AC   D3UY82;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|SAAS:SAAS01097310};
DE            EC=6.3.2.4 {ECO:0000256|SAAS:SAAS01097310};
GN   OrderedLocusNames=XBJ1_0109 {ECO:0000313|EMBL:CBJ79260.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79260.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79260.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79260.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|SAAS:SAAS01097312}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
CC         phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
CC         Evidence={ECO:0000256|SAAS:SAAS01128639};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS01097309};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS01097293};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|SAAS:SAAS01097285}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00595699}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|SAAS:SAAS01087662}.
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DR   EMBL; FN667741; CBJ79260.1; -; Genomic_DNA.
DR   RefSeq; WP_012986727.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0109; -.
DR   EnsemblBacteria; CBJ79260; CBJ79260; XBJ1_0109.
DR   GeneID; 8829733; -.
DR   KEGG; xbo:XBJ1_0109; -.
DR   PATRIC; fig|406818.4.peg.96; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000059197; -.
DR   OMA; CRFDFIV; -.
DR   BioCyc; XBOV406818:XBJ1_RS00485-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002045; 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; 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   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UY82.
DR   SWISS-2DPAGE; D3UY82.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00490552};
KW   Cell shape {ECO:0000256|SAAS:SAAS00140974};
KW   Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS00446019};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS01097289};
KW   Ligase {ECO:0000256|SAAS:SAAS00446140, ECO:0000313|EMBL:CBJ79260.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS01097296};
KW   Manganese {ECO:0000256|SAAS:SAAS01097294};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01097287};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00490618};
KW   Peptidoglycan synthesis {ECO:0000256|SAAS:SAAS00141228};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN      144    348       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   365 AA;  41554 MW;  1B81D2283C625853 CRC64;
     MVYFPSDTKT TIPLSIIFGG ISPEHPASVS SFDNLIKSFR ELNFDRNLNS IYFFDKDGSV
     LYNAYTPYIS PYDFTHSGDK IDLYTAIKRM SKQSEFHINL LHGNLGEDGH IQGVAKYFKI
     KGTFGSVLPS SLSMSKYHMS HYINSLLPSL RSPKTLLLTE GNLEKAFSLI SDNFPEEKIV
     IKPNSLGASL FTNKYVNLEN EKKSILDNLK NIFEYDRFAL VQAFIKGKEY SVGCIRIEGK
     AIALNVVEII TKNGFFGHDE KHRINKAEEI LLIQDSEITR TLKDLSIKIF ESTGYEFMCR
     FDFIVTESEE IYFLESNPIP GMMKNSIFPK MLKGHKLSIP GLFIHLSCSS QNISEKKSIF
     NYIIE
//