ID A0A0G1FXB8_9BACT Unreviewed; 334 AA.
AC A0A0G1FXB8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=D-alanine-D-alanine ligase {ECO:0000313|EMBL:KKT26783.1};
GN ORFNames=UW11_C0006G0049 {ECO:0000313|EMBL:KKT26783.1};
OS Parcubacteria group bacterium GW2011_GWA2_43_9b.
OC Bacteria.
OX NCBI_TaxID=1618828 {ECO:0000313|EMBL:KKT26783.1, ECO:0000313|Proteomes:UP000034814};
RN [1] {ECO:0000313|EMBL:KKT26783.1, ECO:0000313|Proteomes:UP000034814}
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:KKT26783.1}.
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DR EMBL; LCHB01000006; KKT26783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1FXB8; -.
DR STRING; 1618828.UW11_C0006G0049; -.
DR Proteomes; UP000034814; 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; 3.40.50.20; -; 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 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:KKT26783.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 115..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 334 AA; 37447 MW; FDB749761F875190 CRC64;
MKRVIVLYNL AERLEKGVPS DLICEQEITI IVPLVVELLK KRGYQVEALK ADLNLWEELK
ARKGSFDIVF NLAEAFGGGN TNETVVPAML EGLSIPFTGA SLGNMSLILD KEKTKLVLAP
YGIPTAQHVL FRTGREVLNG LGFPLIVKPI KEEASIGIYS DCVVNNEADL LRKVLDSLAK
YKQPIMAERF IRGREISVGV VGNLPDIHVF PPLEFLFEGA TSELEKIRSY EYKWGGKKEQ
MVRADLPPQI IRQLVEYSKI CFEATDCRDY ARMDYRIDPE NGIYLLEVNY NPGIGPNSHG
LNNTLTKMAS FEGCSFEDLV ERVILVAMQR YGLA
//
