ID L0DN96_SINAD Unreviewed; 350 AA.
AC L0DN96;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=ATP-grasp enzyme, D-alanine-D-alanine ligase {ECO:0000313|EMBL:AGA30300.1};
GN OrderedLocusNames=Sinac_6202 {ECO:0000313|EMBL:AGA30300.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA30300.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA30300.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) 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; CP003364; AGA30300.1; -; Genomic_DNA.
DR RefSeq; WP_015249386.1; NZ_JH621481.1.
DR AlphaFoldDB; L0DN96; -.
DR STRING; 886293.Sinac_6202; -.
DR KEGG; saci:Sinac_6202; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_2_0_0; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000010798; Chromosome.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 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:AGA30300.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000010798}.
FT DOMAIN 118..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 350 AA; 36468 MW; E17C32B61052D5F2 CRC64;
MTSVRLKVAV LYNAPVLPPE HPDAVSESDV VGVAQAVVAS FEAQGWDARL LAASPPVVDV
LHNLDRLAPD VVFNLIEGFG GSTAAATHMT GLLELAGYPY TGSPLEALAL CVSKGRAKCL
LRGAGLPTAP GFVMELGASV PRWDWSGPAI VKPDAEDGSL GIDQASVVLD WNSACARVAW
IHATYGGSAL VEAYLPGPEY NVGVLALPEP VALPIAEVAY ESVEGTWPIL TYAAKWSVGS
AEDRASPVSC PARIERELAE SMAGLAVSAF KVTGCRDYAR VDLRLDGRGE PIILEVNPNP
DIGPTAGWAR ALRASGRDYA ATLAALASQA VERARATGAP LRAPDLGSRG
//
