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Database: UniProt
Entry: A0A081BP57_9BACT
LinkDB: A0A081BP57_9BACT
Original site: A0A081BP57_9BACT 
ID   A0A081BP57_9BACT        Unreviewed;       331 AA.
AC   A0A081BP57;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=D-alanine--D-alanine ligase domain protein {ECO:0000313|EMBL:GAK52173.1};
GN   ORFNames=U14_03424 {ECO:0000313|EMBL:GAK52173.1};
OS   Candidatus Moduliflexus flocculans.
OC   Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC   Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX   NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK52173.1};
RN   [1] {ECO:0000313|EMBL:GAK52173.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA   Hugenholtz P.;
RT   "First genomic representation of candidate bacterial phylum KSB3 points to
RT   enhanced environmental sensing as a trigger of wastewater bulking.";
RL   PeerJ 3:e740-e740(2015).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; DF820458; GAK52173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A081BP57; -.
DR   STRING; 1499966.U14_03424; -.
DR   HOGENOM; CLU_039268_2_0_0; -.
DR   Proteomes; UP000030700; 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   Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:GAK52173.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030700}.
FT   DOMAIN          110..325
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   COILED          154..181
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   331 AA;  36710 MW;  821BB495A2E085DD CRC64;
     MKNIVILYGE LPQNAHKDDM DTLAQVKAIS EVLRDAGYSV TPVMLSLNLQ AAKDRLREIQ
     PDLVFNLVES VAGHGRLIYL GTALLDALKI PYTGVHTDAM FITSNKLLAK QRFQSANIPT
     PMWFTREQLR SGAQIPPERY IMKSVWEHAS IGLSEASIRQ TNQAEELCQA LEQQQAELGG
     EGFAETYIDG REFNLSLLAD SDGTPTVLPI AEIVFQGYDN GKAKIVDYRA KWEESSFEYV
     NTVRAFDTLA EDDPLNRRLQ IIALDCWYAF GLRGYARVDF RVSDAGEPFV LEVNANPCLS
     PDAGFAAAAV RAGVTYRETL VRIIAAGSLN E
//
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