ID A0A1G0T378_9BACT Unreviewed; 353 AA.
AC A0A1G0T378;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:OGU79083.1};
GN ORFNames=A2W11_09230 {ECO:0000313|EMBL:OGU79083.1};
OS Ignavibacteria bacterium RBG_16_35_7.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798434 {ECO:0000313|EMBL:OGU79083.1, ECO:0000313|Proteomes:UP000178403};
RN [1] {ECO:0000313|EMBL:OGU79083.1, ECO:0000313|Proteomes:UP000178403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGU79083.1}.
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DR EMBL; MHAG01000232; OGU79083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0T378; -.
DR Proteomes; UP000178403; 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:OGU79083.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 131..342
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 353 AA; 40226 MW; 8B637A36B4F3462B CRC64;
MKAKLKVAII FNEPNPELYR KPSIKFKKPQ NFIPFFEVDQ TTPMEDYKYI QAKLVEEGFD
GYTLNLFDDI NILITDVKKN QPDVIFNFVE LYKDNARLEM NVVGLFELMG IAYTGSPPLA
LANCQNKVMA KKLLNINGIK TPPYFLAADL PEKLKHDLKY PLMVKPAYED ASVGIENESI
VKNKTELLSR MEHVIQNFTQ PVLIEEFIEG RELNIAVFQD EGTRVLPISE IDFTEMPDHL
HNIVSYQAKW DPQHESYHKT IPICPANLPK KIEARAKEIA INAFNVMGCR DYARVDVRLS
ADEEIFVLEV NPNPDLTEGA GFMRSAESAG MTYSQVLKKI VDMAYARKGQ VSL
//
