ID   F7YTY1_9THEM            Unreviewed;       306 AA.
AC   F7YTY1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:AEH51563.1};
DE            EC=6.3.2.4 {ECO:0000313|EMBL:AEH51563.1};
GN   ORFNames=Theth_1510 {ECO:0000313|EMBL:AEH51563.1};
OS   Pseudothermotoga thermarum DSM 5069.
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Pseudothermotoga.
OX   NCBI_TaxID=688269 {ECO:0000313|EMBL:AEH51563.1, ECO:0000313|Proteomes:UP000006804};
RN   [1] {ECO:0000313|EMBL:AEH51563.1, ECO:0000313|Proteomes:UP000006804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5069 {ECO:0000313|EMBL:AEH51563.1,
RC   ECO:0000313|Proteomes:UP000006804};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermotoga thermarum DSM 5069.";
RL   Submitted (NOV-2010) 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; CP002351; AEH51563.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7YTY1; -.
DR   STRING; 688269.Theth_1510; -.
DR   KEGG; tta:Theth_1510; -.
DR   PATRIC; fig|688269.3.peg.1558; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_2_0_0; -.
DR   Proteomes; UP000006804; 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: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:AEH51563.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006804}.
FT   DOMAIN          94..297
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   306 AA;  34914 MW;  A9F39B1BA74A9375 CRC64;
     MIKVAVVFDM VNLDEERKRM IDAVASALSK KFEVEKLPFD DDFVKKVKKF DAVFNLSTAY
     KQIHVPAILD VLNIPYTGSD ALAHALCIDK VITKTILVQN NVPTPEFVAV EVGQLPPQID
     FYPAIVKPSR QGSAKGIHAD SVVHNYDELC RIVKRVHEQF NEPALVEKFI EGKELSVGIV
     AGEVLPILEI DFSELGEGLE RFYSYRVKHY YGDKTKYYCP ARIDETVRKK IEFYAKRAFE
     ALRLKNYARM DLRLKDDEIY FLEVNSLPML TPGYSDIIKM AEATGYSYDE LILKIFEDGV
     MKCFGT
//