ID   F8CL80_MYXFH            Unreviewed;       359 AA.
AC   F8CL80;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=D-ala D-ala ligase domain-containing protein {ECO:0000313|EMBL:AEI65205.1};
GN   OrderedLocusNames=LILAB_16510 {ECO:0000313|EMBL:AEI65205.1};
OS   Myxococcus fulvus (strain ATCC BAA-855 / HW-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI65205.1, ECO:0000313|Proteomes:UP000000488};
RN   [1] {ECO:0000313|EMBL:AEI65205.1, ECO:0000313|Proteomes:UP000000488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488};
RX   PubMed=21868801; DOI=10.1128/JB.05516-11;
RA   Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.;
RT   "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW-
RT   1.";
RL   J. Bacteriol. 193:5015-5016(2011).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CP002830; AEI65205.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8CL80; -.
DR   STRING; 483219.LILAB_16510; -.
DR   KEGG; mfu:LILAB_16510; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_2_0_7; -.
DR   Proteomes; UP000000488; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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   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   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Ligase {ECO:0000313|EMBL:AEI65205.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          114..324
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          330..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   359 AA;  39075 MW;  8302559B06493297 CRC64;
     MHIILLHNRD HDLLEDDPGR EAREDVVRVV SSLADALNQG DTLAEPLAIE GDRLDFVDTL
     RRRQPDLVVN LCESLAADSR GEMAVPCLLD ALGLAYTGSS ALSLGLALHK PKAKEVLTAR
     GVSTPPFRVV ERLEDALAVD LPWPLIVKPA REDASMGVTS ESVVHERAAL VRACDAVLRE
     FHQPALVEQF IPGREIYVPL LGNQPRQALP LTEIVFGRTF EDRPNIVSYN AKWEAASAEY
     RDTTSGLCRL DANLESRCVQ VALEAFAALD CQDYGRVDLR VSPEGVPYVI DINPNCDLHP
     SAGFAKAALA AGMDYPALAS RLVEVALERA HGHPSHRRKG PGADRRADSK DRNLLAAGG
//