ID A0A0S8K390_9BACE Unreviewed; 650 AA.
AC A0A0S8K390;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:KPL16406.1};
GN ORFNames=AMS26_04720 {ECO:0000313|EMBL:KPL16406.1};
OS Bacteroides sp. SM23_62.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL16406.1, ECO:0000313|Proteomes:UP000050819};
RN [1] {ECO:0000313|EMBL:KPL16406.1, ECO:0000313|Proteomes:UP000050819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_62 {ECO:0000313|EMBL:KPL16406.1};
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:KPL16406.1}.
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DR EMBL; LJUP01000028; KPL16406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8K390; -.
DR PATRIC; fig|1703352.3.peg.1818; -.
DR Proteomes; UP000050819; 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 CDD; cd02440; AdoMet_MTases; 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 Gene3D; 2.20.25.110; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_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 Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:KPL16406.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 409..623
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 650 AA; 74636 MW; 78927B18EF6E0549 CRC64;
MKNKKSCKIA AQSFGPVHNL EEFLQPDWWR RIFNSMYLKT DADVVEDESI TGIELDMFTT
LMNLSSEDVI LDLACGQGRH SLELARRGFK NIYGLDRSHY LVNKAKQICF NEGLSVSFKE
GDARKLPYPV DHFDVVMILG NSFGYFESID DDIQVLNEVL RVLKPHGKFL MDVADGNFLK
TNFNPRSWEW MDKNHFVCRE RSLSSDNDRM ISREVISHTK KGVIVDQFYA ERLYSRDKLT
EILENAGFRN IRIHDNYTTN SSRNQDLGMM EQRIILSAEV VKDWSPLKKE HAGLTRVVVL
LGDPSKTDIV KPDTLFDEDD YITIEELKTA LGSLKNYKFT YLDNHDMLIN NLIKLRPEID
IVLNLCDEGF NNNPRSELHI PSLLEILNIP YSGSNPQCLA YCYDKSLIRG IAKEMDIPVA
DALYINPVDN VIELNIEFPV IAKPNFGDSS FGITQKSVAY TVEELNDAIV KTRMRFGYDK
PILVEEFLTG KDLSLGIIGN PPESYTILPI IEEDYSQLPE GLPRICGYEA KWLQDSAYFK
LLRSIKADLD IETEKKIVSW SLNMTERLEC RDYVRFDWRL DENGSPKLLE INPNPGWCWD
GHLAKMASLK GFTYATMLQE ILIATEQRVG EHLVSNRVKE HTTVSLHTDF
//
