ID   Q30WW0_OLEA2            Unreviewed;       349 AA.
AC   Q30WW0;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:ABB39836.1};
DE            EC=6.3.2.4 {ECO:0000313|EMBL:ABB39836.1};
GN   OrderedLocusNames=Dde_3042 {ECO:0000313|EMBL:ABB39836.1};
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559 {ECO:0000313|EMBL:ABB39836.1, ECO:0000313|Proteomes:UP000002710};
RN   [1] {ECO:0000313|EMBL:ABB39836.1, ECO:0000313|Proteomes:UP000002710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA 1058 / DSM 17464 / G20
RC   {ECO:0000313|Proteomes:UP000002710};
RX   PubMed=21685289; DOI=10.1128/JB.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(2011).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CP000112; ABB39836.1; -; Genomic_DNA.
DR   RefSeq; WP_011368807.1; NC_007519.1.
DR   AlphaFoldDB; Q30WW0; -.
DR   STRING; 207559.Dde_3042; -.
DR   KEGG; dde:Dde_3042; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_2_1_7; -.
DR   Proteomes; UP000002710; Chromosome.
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:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Ligase {ECO:0000313|EMBL:ABB39836.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002710}.
FT   DOMAIN          113..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   349 AA;  37500 MW;  19B104561BAB9FE6 CRC64;
     MLVGITYDLK EEYLARGYSE EEAAEFDSPA TIEGIETALQ ALGYETQRIG ALPALAAALL
     QGRRWDIVFN IAEGCHGFGR ESQVPALLDY YSVPYVFSDP MTLGICLHKG MTKHIVRDNG
     IPTADFVVIS DPAEAAAVSL PYPLFVKPVA EGTGIGVGAA SKVQNPQELA AACARLIDRH
     RQPVLVETFL CGRELTVGIT GTGAGARTLG ALEVVFAPAA ESDVYGYVNK AEYLERVQYH
     LADDADAQKA RHVALAAWRA LGCRDGGRVD LRFDARGVPN FIEVNPLAGL NPVNSDLPIM
     CYKAGLRYEQ LIGQIMESAV ERLKTDTGQR FVPAVTAAAY TGHTGTVAE
//