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Database: UniProt
Entry: A0A0S8AZD5_9PROT
LinkDB: A0A0S8AZD5_9PROT
Original site: A0A0S8AZD5_9PROT 
ID   A0A0S8AZD5_9PROT        Unreviewed;       171 AA.
AC   A0A0S8AZD5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:KPK04831.1};
DE   Flags: Fragment;
GN   ORFNames=AMJ64_12725 {ECO:0000313|EMBL:KPK04831.1};
OS   Betaproteobacteria bacterium SG8_39.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1703390 {ECO:0000313|EMBL:KPK04831.1, ECO:0000313|Proteomes:UP000051483};
RN   [1] {ECO:0000313|EMBL:KPK04831.1, ECO:0000313|Proteomes:UP000051483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_39 {ECO:0000313|EMBL:KPK04831.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPK04831.1}.
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DR   EMBL; LJTQ01000143; KPK04831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8AZD5; -.
DR   STRING; 1703390.AMJ64_12725; -.
DR   Proteomes; UP000051483; Unassembled WGS sequence.
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   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
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:0000313|EMBL:KPK04831.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          26..165
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KPK04831.1"
SQ   SEQUENCE   171 AA;  19255 MW;  DD45046BBD1C5F89 CRC64;
     ASVVYNDEKL VERVAFMHEK IGSDAILEQY IDGRELYVGV IGNHRLRVLP PLELSIGKLR
     SDAPRIATRR VKWDSAYQAR RDVKLEPAKD LAPEVVRTLL QVTKRAYRLL GLSGYARMDF
     RLGADNRPYF LEANPNPDIA REAELAEAAG LDGLDYPALL DRVLRVGLAT R
//
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