ID A0A0S7XCW4_9BACT Unreviewed; 636 AA.
AC A0A0S7XCW4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:KPJ60258.1};
GN ORFNames=AMJ46_07405 {ECO:0000313|EMBL:KPJ60258.1};
OS Latescibacteria bacterium DG_63.
OC Bacteria; Candidatus Latescibacteria.
OX NCBI_TaxID=1703781 {ECO:0000313|EMBL:KPJ60258.1, ECO:0000313|Proteomes:UP000051457};
RN [1] {ECO:0000313|EMBL:KPJ60258.1, ECO:0000313|Proteomes:UP000051457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_63 {ECO:0000313|EMBL:KPJ60258.1};
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:KPJ60258.1}.
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DR EMBL; LJNC01000012; KPJ60258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7XCW4; -.
DR PATRIC; fig|1703781.3.peg.1546; -.
DR Proteomes; UP000051457; 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 GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.20; -; 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; 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; IPR041698; Methyltransf_25.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
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; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 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 Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000313|EMBL:KPJ60258.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 396..609
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 636 AA; 73030 MW; CC59A300BB302948 CRC64;
MGPVSSLEEH VHADWWRRIF GSVYLKTDAD VIDDQRITAK EVDLFGEILK LTPEDRVLDL
CCGQGRHSLE LVRRGVRNVE GLDRSHYLIQ KARSQARKEG LTIRFREGDA RKLPYPADTF
SAVMILGNSF GYFETAQDDM RVLREVQKVL KPWGRVLIDV ADGKYLRREF QPRSWEWIDK
KQFVCRERCL SVDGQRLISR EVVTHVEKGV VADHFYAERL YSRQSLTELL EAAGFSDVTF
HGEISPESER NQDLGMMERR IVATAVVRKE WSPVRRRKEQ ASHIVVVLGD PTKPDLLKPS
KVFDEDDIYT IDQLKSALRD MQDYQFTYLD NHDTLIQDLL RAKPKIDMVF NLCDEGFSND
ATRELHVPSL LEVLGIPYTG AGPQCLAYCY DKSLVRGIAK EMEIPVPEAF FIKPEDKAFE
LPFAFPVIVK PNVGDSSFGI TQRSVCHSIE QLVDAISEIR ERFGYEKPIL VEEFLTGKDL
SLGIIGNPPE SYRTLPIIEE DYSTLPPELP RICGYEAKWM PDSPYWKIRS IPAELPDETE
KLIIEWCLKL FERLECRDYC RFDWRLDGAG NPKLLEVNPN PGWCWDGHLA KMAKTVDIPY
AEMLDGILRA AEQRLRLQSS RGEREENAAA DPPIST
//
