ID A0A1G2S9G4_9BACT Unreviewed; 319 AA.
AC A0A1G2S9G4;
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=A2675_03785 {ECO:0000313|EMBL:OHA81716.1};
OS Candidatus Yonathbacteria bacterium RIFCSPHIGHO2_01_FULL_51_10.
OC Bacteria; Candidatus Yonathbacteria.
OX NCBI_TaxID=1802723 {ECO:0000313|EMBL:OHA81716.1, ECO:0000313|Proteomes:UP000176997};
RN [1] {ECO:0000313|EMBL:OHA81716.1, ECO:0000313|Proteomes:UP000176997}
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:OHA81716.1}.
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DR EMBL; MHUS01000008; OHA81716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2S9G4; -.
DR STRING; 1802723.A2675_03785; -.
DR Proteomes; UP000176997; 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..313
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 319 AA; 34662 MW; 338463ED7C27DA67 CRC64;
MTSMRVGVMR GGISDEYDIS LKTGGAVLKV LAENGGKPRD ILITKDGTWH LDGVPVVPEN
IARQVDVMWN GLHGEYGEDG KVQQLLETLK VPYTGSRPFA SALGMNKQLS KRRFLDAGLL
TPQGFVVNRG ERGEDTARSI FQKMAPPYIV KPLTGGSSIG VVMARTPGQL AALIAGLLAS
SESIIVEEYI RGREVVAGAV EVGDGMIHSL RPLSVTLPDG EHVFTQNLKH SPGDLYAPVE
SRAQHDDIAY AMRTLARELS IRHYFTADFI SSPHGLYILE VNTLPGLSST SAFSRMLHEQ
DSNLGEFVEH MLLLALEGK
//
