ID A0A1I5RT98_9BRAD Unreviewed; 330 AA.
AC A0A1I5RT98;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:SFP61627.1};
GN ORFNames=SAMN05216330_108304 {ECO:0000313|EMBL:SFP61627.1};
OS Bradyrhizobium sp. Ghvi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855319 {ECO:0000313|EMBL:SFP61627.1, ECO:0000313|Proteomes:UP000198509};
RN [1] {ECO:0000313|EMBL:SFP61627.1, ECO:0000313|Proteomes:UP000198509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ghvi {ECO:0000313|EMBL:SFP61627.1,
RC ECO:0000313|Proteomes:UP000198509};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; FOVU01000008; SFP61627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5RT98; -.
DR STRING; 1855319.SAMN05216330_108304; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000198509; 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:SF23; D-ALANINE--D-ALANINE LIGASE B; 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 Ligase {ECO:0000313|EMBL:SFP61627.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 129..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 330 AA; 35923 MW; 3595D07642D02CA3 CRC64;
MNMRTTILFG GSNRERLVSV ASAQALQQAL PEADLWFWDV EDKVHLVQPK QLLEHSRPFE
DEFKPGTRGI PLAQALDQAK VEDRVLVLSL HGGCAENGEL QVMCEARGVP FTGSGSASSH
LAFDKIAAKR FAALGGVTPP AGIALEDIDD AFAEYGRLIA KPARDGSSYG LIFVNARQDL
VAVRNAAKHE DYVIEPYIAG VEATCGVLER TDGSIISLPP IEIIPGEGNF DYAAKYLLST
TQEICPGRFT PEVTAALKRQ AMLAHRAMSC SGYSRSDFIV SEKGLVYLET NTLPGLTKSS
LYPKALKAEG IAFVDFLRDL IELAVRRVRK
//
