ID Q9ZFK2_PAEPP Unreviewed; 158 AA.
AC Q9ZFK2;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE SubName: Full=Putative D-alanine:D-alanine ligase {ECO:0000313|EMBL:AAC83823.1};
DE Flags: Fragment;
OS Paenibacillus popilliae (Bacillus popilliae).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=78057 {ECO:0000313|EMBL:AAC83823.1};
RN [1] {ECO:0000313|EMBL:AAC83823.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ch1 {ECO:0000313|EMBL:AAC83823.1};
RA Eirikis E., Knob C., Dingman D., Fraimow H.S.;
RT "Characterization of vancomycin resistance in Bacillus popilliae.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAC83823.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ch1 {ECO:0000313|EMBL:AAC83823.1};
RX PubMed=15980329; DOI=10.1128/AAC.49.7.2625-2633.2005;
RA Fraimow H., Knob C., Herrero I.A., Patel R.;
RT "Putative VanRS-like two-component regulatory system associated with the
RT inducible glycopeptide resistance cluster of Paenibacillus popilliae.";
RL Antimicrob. Agents Chemother. 49:2625-2633(2005).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; AF098802; AAC83823.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZFK2; -.
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 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 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 SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AAC83823.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 26..122
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAC83823.1"
FT NON_TER 158
FT /evidence="ECO:0000313|EMBL:AAC83823.1"
SQ SEQUENCE 158 AA; 17700 MW; 42A4708475146F7E CRC64;
RSRWRFPYVG AGVLASSVGM DKAIMKHVFA HAGLPQCKYE HFLRREWDQN QAEILDRVQT
ELGYPCFVKP ANLGSSVGIS KARNAAELKQ AIELALQYDR KIIVEEFVDA REVEVSVLGN
DEPQASIPGE IISSNEFYDY KAKYIDGKSQ IAIPAPLD
//
