ID M1NA13_DESSD Unreviewed; 328 AA.
AC M1NA13;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=ATP-grasp enzyme, D-alanine-D-alanine ligase {ECO:0000313|EMBL:AGF76694.1};
DE EC=6.3.2.4 {ECO:0000313|EMBL:AGF76694.1};
GN OrderedLocusNames=UWK_00107 {ECO:0000313|EMBL:AGF76694.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF76694.1, ECO:0000313|Proteomes:UP000011721};
RN [1] {ECO:0000313|Proteomes:UP000011721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; CP003985; AGF76694.1; -; Genomic_DNA.
DR RefSeq; WP_015402393.1; NC_020304.1.
DR AlphaFoldDB; M1NA13; -.
DR STRING; 1167006.UWK_00107; -.
DR KEGG; dsf:UWK_00107; -.
DR PATRIC; fig|1167006.5.peg.119; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_2_1_7; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000011721; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-EC.
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; 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.
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:AGF76694.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT DOMAIN 113..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 328 AA; 36077 MW; E8E718EF559D4C16 CRC64;
MKIGLTFDLR SAYLEMGFSE LETAEFDRDD TITAIENALT TLGHKCERIG HARQLMQALT
EGKRWDLVFN IAEGMYGIGR EAQIPAILDV FNIPYTFSDP LVMSLTLHKG MTKRVLRDAK
VAVSDFLVAE KGSEAAAISF GGPWFIKPVA EGTGKGIDPT SIVRDKAELP GAVDHLIEKF
KQPVIIEPYL PGREFTVGIV GTGNVAKVLG TIEVVLLQNA EEGVYSYVNK EECEERVEYR
LVHGSKDPVV KEAENTALEA WRVLGCRDGG RADLRCNANG KPLFMEVNPL AGIHPQHSDL
PILCTMQNID YLSLVEMILT SASARVTL
//
