ID W3RRD4_9BRAD Unreviewed; 329 AA.
AC W3RRD4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:ETR78854.1};
GN ORFNames=X566_15230 {ECO:0000313|EMBL:ETR78854.1};
OS Afipia sp. P52-10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1429916 {ECO:0000313|EMBL:ETR78854.1, ECO:0000313|Proteomes:UP000018975};
RN [1] {ECO:0000313|Proteomes:UP000018975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P52-10 {ECO:0000313|Proteomes:UP000018975};
RX PubMed=25874801;
RA Pickering B.S., Tyler S., Smith G., Burton L., Li M., Dallaire A.,
RA Weingartl H.;
RT "Identification of a novel afipia species isolated from an Indian flying
RT fox.";
RL PLoS ONE 10:E0121274-E0121274(2015).
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}.
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:ETR78854.1}.
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DR EMBL; AZSJ01000003; ETR78854.1; -; Genomic_DNA.
DR RefSeq; WP_034468800.1; NZ_AZSJ01000003.1.
DR AlphaFoldDB; W3RRD4; -.
DR STRING; 1429916.X566_15230; -.
DR PATRIC; fig|1429916.3.peg.3097; -.
DR eggNOG; COG1181; Bacteria.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000018975; 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:ETR78854.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000018975}.
FT DOMAIN 128..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 329 AA; 35587 MW; AB96AF0430CE03CA CRC64;
MRITILFGGT NKERLVSVAS AQALHTALPD ADLWFWDVDN TVHETSPQAL LAHARPFEEP
FKADGRPLGP IEPALDRAKA EDRLFVFGLH GGMAENGELQ AMCEMRGIAF TGSGSASSYL
AFDKVLAKRF AAIAGVQTLP SVALQDAEAA LGQYGKLIAK PSRDGSSYGL IFVNARQDIV
AVRNASKTED YLIEPFIAGV EATCGVLELA DGSLTALPPI EIIPAEGAFD YTAKYLAKST
QEICPGRFSA EVTTRLMDHA MRAHRVLSCR GYSRSDFIVS DKGLIYLETN TLPGLTKASL
YPKALHAQGV TFVDFLTGQI ELAARHVRR
//
