ID B0K7X8_THEP3 Unreviewed; 325 AA.
AC B0K7X8;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:ABY95798.1};
DE EC=6.3.2.4 {ECO:0000313|EMBL:ABY95798.1};
GN OrderedLocusNames=Teth39_2176 {ECO:0000313|EMBL:ABY95798.1};
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099 {ECO:0000313|EMBL:ABY95798.1, ECO:0000313|Proteomes:UP000002156};
RN [1] {ECO:0000313|Proteomes:UP000002156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E
RC {ECO:0000313|Proteomes:UP000002156};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000924; ABY95798.1; -; Genomic_DNA.
DR RefSeq; WP_012269782.1; NC_010321.1.
DR AlphaFoldDB; B0K7X8; -.
DR STRING; 340099.Teth39_2176; -.
DR KEGG; tpd:Teth39_2176; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_2_0_9; -.
DR Proteomes; UP000002156; 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 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 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 PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABY95798.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000002156}.
FT DOMAIN 105..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 325 AA; 37055 MW; 2D8CE07D05E63AB5 CRC64;
MKIGVLWRKF RNVEFQRKLT PDKVYDDAYD EAYHHYMAIK EAGFDSVLIE WKEDPLETYE
TIKKEKVDLI FNASSMKEVA FLEVFNIPYV GSGLDVVATD KRMRKDIVAS HGLPTPKYVI
AENPQEIPSV DHLKFPLFVK PISGRGSAGI DEENIIYDKD KLPQVVSKIT EKIGQAALIE
EFIEGKEVTV GIIGYKHPQV LPLLEVGYNN VKTNTYEHKM FDNEIIKCPI EVPKEVEEKI
KETALNIYKV LNAKDFARID MILSKDNVPY FLELNTFAGL TMSSSKGEKH VHHGYMGYMA
KAAGLTRGEF IGKIIESAIE RYKLK
//