ID C8C0X0_9ZZZZ Unreviewed; 367 AA.
AC C8C0X0;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative D-alanine-D-alanine ligase {ECO:0000313|EMBL:ACT97553.1};
OS uncultured organism.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=155900 {ECO:0000313|EMBL:ACT97553.1};
RN [1] {ECO:0000313|EMBL:ACT97553.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19713526; DOI=10.1126/science.1176950;
RA Sommer M.O., Dantas G., Church G.M.;
RT "Functional characterization of the antibiotic resistance reservoir in the
RT human microflora.";
RL Science 325:1128-1131(2009).
RN [2] {ECO:0000313|EMBL:ACT97553.1}
RP NUCLEOTIDE SEQUENCE.
RA Sommer M.O.A., Dantas G., Church G.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; GQ343102; ACT97553.1; -; Genomic_DNA.
DR EMBL; GQ343111; ACT97564.1; -; Genomic_DNA.
DR AlphaFoldDB; C8C0X0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0008360; P:regulation of cell shape; 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 HAMAP; MF_00047; Dala_Dala_lig; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR000291; D-Ala_lig_Van_CS.
DR InterPro; IPR005905; D_ala_D_ala.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR011127; Dala_Dala_lig_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01820; Dala_Dala_lig_N; 1.
DR PIRSF; PIRSF039102; Ddl/VanB; 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; PS00843; DALA_DALA_LIGASE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ACT97553.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 169..360
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 367 AA; 40749 MW; AD50C118BC03BAB4 CRC64;
MLYSIRYAQE NYTIRDCVWK RGLIMNIVVL AGGTSTERDI SILTSTKVCE SLRRNGYNAN
IVDVFFGIDS ENVDNFFNND NDLEKLCKYL KNQTPDVEKE LEARKALGKG FFGDNVLELC
QKADIVFMGL HGSNGEDGKI QAAFELMGIK YTGTDYISSA ISMSKELTKK VLVPEGIPMP
KGIALHKGHK VEYVPFPCVV KPCCGGSSVG VSIVNSEEEF KRALTDAFSY EDNILVEEFI
KGREFSVGVL NGKALPVIEI EPLDGFYDYK NKYKAGATKE TCPANLPKEI SEKMQRWAEK
ACETAGVTTY ARVDELLNED GDIYCLEINT LPGMTGTSLL PQEAAAVGMS YDELTKKIIE
ISLEKYN
//
