ID   E8US28_THEBF            Unreviewed;       325 AA.
AC   E8US28;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:ADV80727.1};
DE            EC=6.3.2.4 {ECO:0000313|EMBL:ADV80727.1};
GN   OrderedLocusNames=Thebr_2222 {ECO:0000313|EMBL:ADV80727.1};
OS   Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389 /
OS   AKO-1) (Thermoanaerobacter finnii).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=509193 {ECO:0000313|EMBL:ADV80727.1, ECO:0000313|Proteomes:UP000002062};
RN   [1] {ECO:0000313|EMBL:ADV80727.1, ECO:0000313|Proteomes:UP000002062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43586 / DSM 3389 / AKO-1
RC   {ECO:0000313|Proteomes:UP000002062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter brockii finnii Ako-1.";
RL   Submitted (JAN-2011) 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; CP002466; ADV80727.1; -; Genomic_DNA.
DR   RefSeq; WP_012269782.1; NC_014964.1.
DR   AlphaFoldDB; E8US28; -.
DR   KEGG; tbo:Thebr_2222; -.
DR   HOGENOM; CLU_039268_2_0_9; -.
DR   Proteomes; UP000002062; 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:ADV80727.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
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
//