ID A0A0G1AAK5_9BACT Unreviewed; 350 AA.
AC A0A0G1AAK5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=D-alanine-D-alanine ligase {ECO:0000313|EMBL:KKS31111.1};
GN ORFNames=UU93_C0022G0007 {ECO:0000313|EMBL:KKS31111.1};
OS Candidatus Amesbacteria bacterium GW2011_GWA2_42_12.
OC Bacteria; Candidatus Amesbacteria.
OX NCBI_TaxID=1618356 {ECO:0000313|EMBL:KKS31111.1, ECO:0000313|Proteomes:UP000034160};
RN [1] {ECO:0000313|EMBL:KKS31111.1, ECO:0000313|Proteomes:UP000034160}
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:KKS31111.1}.
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DR EMBL; LCCN01000022; KKS31111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1AAK5; -.
DR STRING; 1618356.UU93_C0022G0007; -.
DR Proteomes; UP000034160; 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 GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR InterPro; IPR011761; ATP-grasp.
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:KKS31111.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 131..334
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 350 AA; 39722 MW; C4936824F75C01B0 CRC64;
MTNTKTDNDE PGGNGSLLPK FVGLIHSEVK REYFPTEMQY ITEKDAEHEA LVIATYLEKM
GIKVKLYPGR PEVVQQLVKD KPEMVFNLVG SISGQDYLTA IIPGMMEAID IPYTGAGMLG
ESLAYNKFLV KQLLQSHGVP TPQSQLMSTP STLLNTDMRF PLITKLNEIH GAVEVTKDAI
SMEEKHLRER VKHLIHTYQQ PVIVEEFVAG REYTAIVLEG LNTKVYIAEK VFPEPDDPMQ
FATFDAQWVT DAVSYKYVKV IDPILTELVK KAFFILKMAG YAKFDIRVDQ AKRYYFVDSN
SNPAFGPKEL DVAMATILDM HDVSFTEILK RLMANTMREW YKTQEETGIM
//
