ID A0A1F6VID9_9BACT Unreviewed; 330 AA.
AC A0A1F6VID9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=A2824_00855 {ECO:0000313|EMBL:OGI69295.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_01_FULL_42_16.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801743 {ECO:0000313|EMBL:OGI69295.1, ECO:0000313|Proteomes:UP000178059};
RN [1] {ECO:0000313|EMBL:OGI69295.1, ECO:0000313|Proteomes:UP000178059}
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:OGI69295.1}.
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DR EMBL; MFTT01000028; OGI69295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6VID9; -.
DR STRING; 1801743.A2824_00855; -.
DR Proteomes; UP000178059; 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; 3.30.1490.20; 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 InterPro; IPR011127; Dala_Dala_lig_N.
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 Pfam; PF01820; Dala_Dala_lig_N; 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 Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 111..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 330 AA; 36795 MW; 8E1C8938E7D2B9FF CRC64;
MKLKVGVLRG GVGPEYDISL KTGGAVLANL DREKYRPVDI LIDKEGIWHA DGIPLKSKEN
LKSIVDVVWN GMHGYLGEDG RIQNFLEGAG VPFTGPRSLP AYVSLNKSLA KNKFSKLGLR
SPFGEMVGDE IEFWNYGGDS ERYVEDKARE IFQKISPPWI VKPLLGTCSI DVYLAENFAE
LVAALTKVLQ NHESALVEEF VRGREIVVGI IENFRDKENY TLIPLEIIKS KPVFDYETRH
GGDYRLLRPA DLTLDEKVLI GEAAAKIHEH FDLGQYSLVD LILTKNGVRV LEVDSLPDLG
EHSLFCRSLA EVGAGVPEFL ECVINKTLEK
//
