ID A0A1G1A3M7_9BACT Unreviewed; 327 AA.
AC A0A1G1A3M7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:OGV65093.1};
GN ORFNames=A2498_13260 {ECO:0000313|EMBL:OGV65093.1};
OS Lentisphaerae bacterium RIFOXYC12_FULL_60_16.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798582 {ECO:0000313|EMBL:OGV65093.1, ECO:0000313|Proteomes:UP000178496};
RN [1] {ECO:0000313|EMBL:OGV65093.1, ECO:0000313|Proteomes:UP000178496}
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:OGV65093.1}.
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DR EMBL; MHBQ01000074; OGV65093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1A3M7; -.
DR STRING; 1798582.A2498_13260; -.
DR Proteomes; UP000178496; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; IPR000291; D-Ala_lig_Van_CS.
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:SF23; D-ALANINE--D-ALANINE LIGASE B; 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.
DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OGV65093.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 113..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 327 AA; 36316 MW; 9238E2720940D0E5 CRC64;
MHIGLVYDLR SDYLAEGYTE EQVAEFDFDA TLDALEKGIR SLGYRTDRIG HARALCSRLV
KGDRWDLVFT IAEGVQGRSR EAQVPCLLEL YGIPYTFSDP LTCAITLDKA ATKRLVQAAG
LPTPAFAVIA KPADCAGVRL RYPLFAKPLA EGTGKGVDTA SRIDTPQALL SVCRRLIRRF
AQPVLVEEYL PGREFTTAVL GTGAAARVLG TMEVRIKADT PTRDYSYAIK EQCEQYVEYG
PPEHGTLRRK VEALALAAHR ALECRDASRS DVRLDHRGRP SFMEINPLPG LHPQHSDLPM
IATQEGMRYR ELLARIIGSA VRRYGLR
//
