ID C8C0Y5_9ZZZZ Unreviewed; 332 AA.
AC C8C0Y5;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Putative D-alanine-D-alanine ligase {ECO:0000313|EMBL:ACT97568.1};
OS uncultured organism.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=155900 {ECO:0000313|EMBL:ACT97568.1};
RN [1] {ECO:0000313|EMBL:ACT97568.1}
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:ACT97568.1}
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; GQ343114; ACT97568.1; -; Genomic_DNA.
DR AlphaFoldDB; C8C0Y5; -.
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:ACT97568.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 125..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 332 AA; 37206 MW; 37ADF98F50A87C8A CRC64;
MKNLKRTIAI VCGGDSSEHD VSLRSAQGLY SFFDKERYDV YIVDVRGTDW RVQLPDGEEA
KIDRNDFSFV KTDGTAVVFD YAYITIHGQP GENGPMQGYF DLIHVPYSTS GVLVEAMTFD
KFVLNRYLGS FGIHVADSVL LRRGETYNEE EIAKRIGMPC FVKPANDGSS FGVSKVKNAD
QLEPALRVAF MESSDVMVEA YLDGTEITQG IYKTRERSVP FPITEVVTTN EFFDYDAKYN
GQVDEITPAR ISPETAERVT EITSRIYDIL HANGIIRIDY IITHDAEGNE VINMLEVNTT
PGMTTTSFIP QQVRAAGLDI KDVLTEIIEN QL
//
