ID A0A0G1K425_9BACT Unreviewed; 363 AA.
AC A0A0G1K425;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=D-ala D-ala ligase domain-containing protein {ECO:0000313|EMBL:KKT78243.1};
GN ORFNames=UW73_C0005G0068 {ECO:0000313|EMBL:KKT78243.1};
OS Microgenomates group bacterium GW2011_GWB1_44_8.
OC Bacteria.
OX NCBI_TaxID=1618505 {ECO:0000313|EMBL:KKT78243.1, ECO:0000313|Proteomes:UP000034467};
RN [1] {ECO:0000313|EMBL:KKT78243.1, ECO:0000313|Proteomes:UP000034467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKT78243.1}.
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DR EMBL; LCJL01000005; KKT78243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1K425; -.
DR STRING; 1618505.UW73_C0005G0068; -.
DR Proteomes; UP000034467; Unassembled WGS sequence.
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:KKT78243.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 121..335
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 363 AA; 41023 MW; BE57DC367DFB9CE4 CRC64;
MSNRVRFKEK PQKVTIIYNS VDESSPFSPL DRRVADADTI NMAIDIAGNL EKVFETDLID
IPLDHPESVS SIKTDIVFNL CEGVGYEFAC KVIDSLESAH IPYIGANSLN YHIGSDKALL
KEVLNRFGLP TPAGQYFENP ADKVKPSLKF PLLIKPEFEH GSVGITQESV VKDVSQLKEQ
ILRIKNEYKQ GVLVEEYIDG MELQLTLVGN GESLLVLPIK EILFVNGMSN RWHVVTFSAK
WEEDSDEYKG TPTICPTENL DDDEKTVLEK LGREIFIKTD CQDYTRIDIR YDKKSKTPYI
LDVNPNPDLS SDAAVAKAAQ AIGWDYQTLL TQLVIAAWER VTRAPRPVDK RETLLCHRPY
DNQ
//
