ID A0A1Q7RN15_9BACT Unreviewed; 298 AA.
AC A0A1Q7RN15;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
DE Flags: Fragment;
GN ORFNames=AUI33_11545 {ECO:0000313|EMBL:OLD65394.1};
OS Ignavibacteria bacterium 13_1_40CM_2_61_4.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1805219 {ECO:0000313|EMBL:OLD65394.1, ECO:0000313|Proteomes:UP000186155};
RN [1] {ECO:0000313|EMBL:OLD65394.1, ECO:0000313|Proteomes:UP000186155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(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:OLD65394.1}.
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DR EMBL; MNHF01001167; OLD65394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7RN15; -.
DR Proteomes; UP000186155; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005905; D_ala_D_ala.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR011127; Dala_Dala_lig_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF25; D-ALANINE--D-ALANINE LIGASE A; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01820; Dala_Dala_lig_N; 1.
DR PIRSF; PIRSF039102; Ddl/VanB; 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 165..261
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 298
FT /evidence="ECO:0000313|EMBL:OLD65394.1"
SQ SEQUENCE 298 AA; 32177 MW; DFEE9DD4141E7ABF CRC64;
MRTRKKETRG RAGHGHARLR VGVIYGGRSV EHEVSLVSAR AIMQALDPRR YEVVPIGITR
QGRWVLAGAH WTLPPDPSVR GLVRLRNGGR AGTALASLPR AALRSAAGPG RDPGPLGRLD
VIFPVVHGMG GEEGTLQGLL ELADIPYVGA GVLGSALGMD KAMMKVVFRE AGLPIVDHRV
LRRSDLEAGR DRFVQAVEEA FGYPCFVKPA NGGSSVGVSK AKRRADLLEA IDLAARYDRK
IIVERGVDAR EIECSVLGND EPEASVPGEI VPGNEFYDYR AKYIDENSRL LIPAPLSP
//
