ID A0A101FUK2_9EURY Unreviewed; 335 AA.
AC A0A101FUK2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:KUK44627.1};
GN ORFNames=XD72_0999 {ECO:0000313|EMBL:KUK44627.1}, XE07_1557
GN {ECO:0000313|EMBL:KUK95836.1};
OS Methanothrix harundinacea.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=301375 {ECO:0000313|EMBL:KUK44627.1, ECO:0000313|Proteomes:UP000057043};
RN [1] {ECO:0000313|Proteomes:UP000053961, ECO:0000313|Proteomes:UP000057043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=57_489 {ECO:0000313|EMBL:KUK44627.1};
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
RN [2] {ECO:0000313|EMBL:KUK95836.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56_747 {ECO:0000313|EMBL:KUK95836.1};
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-resolved metagenomic analysis reveals roles for candidate phyla and
RT other microbial community members in biogeochemical transformations in oil
RT reservoirs.";
RL MBio 7:e01669-15(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:KUK44627.1}.
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DR EMBL; LGFT01000020; KUK44627.1; -; Genomic_DNA.
DR EMBL; LGHB01000025; KUK95836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101FUK2; -.
DR PATRIC; fig|301375.6.peg.721; -.
DR Proteomes; UP000053961; Unassembled WGS sequence.
DR Proteomes; UP000057043; 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 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 InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 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:KUK44627.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 112..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 335 AA; 37142 MW; 618E3DE60406256E CRC64;
MKVALTCNTL PPDYSRESGD DTFAEFDSPS TISAIKKALL THCDSVEVVE ADEEAYERLR
RGNFDFAFNI AEGVRGEARE AQIPAMLEML GIPYSGSGVT TLAITLDKRR TKEVLLANGI
RTPKFQLLSR SEDLRSDLKF PLFLKPNGEG SSRGITARSL VGSEEELEEV AREMVAKYRQ
PVLVEEYLTG REFTVGLLGN PPEVLPVVEV GFEGLPPGAP KFDCYEVKWI YDSLEARYDT
TVCPARVDDD LRSRIADTAT RTFEALEVRD LCRLDLRLDG DGEPSVFDVN ALPGLIPDPA
ENSRFPKAAY AAGYSYEELI GEVFNAALRR EGILR
//
