ID A0A0G1M8G1_9BACT Unreviewed; 723 AA.
AC A0A0G1M8G1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
DE Flags: Fragment;
GN ORFNames=UW70_C0002G0001 {ECO:0000313|EMBL:KKT77162.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWA2_44_7.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619057 {ECO:0000313|EMBL:KKT77162.1, ECO:0000313|Proteomes:UP000034415};
RN [1] {ECO:0000313|EMBL:KKT77162.1, ECO:0000313|Proteomes:UP000034415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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:KKT77162.1}.
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DR EMBL; LCJI01000002; KKT77162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1M8G1; -.
DR STRING; 1619057.UW70_C0002G0001; -.
DR Proteomes; UP000034415; 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; -; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR011127; Dala_Dala_lig_N.
DR InterPro; IPR016185; PreATP-grasp_dom_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; PF01820; Dala_Dala_lig_N; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
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 Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 134..346
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 723
FT /evidence="ECO:0000313|EMBL:KKT77162.1"
SQ SEQUENCE 723 AA; 82047 MW; 321E4DF7379B81F5 CRC64;
MKKLKVALIC GGPSLERGIS LNSARSVLDH LAGPDIEIVP IYFDHKKRPY HISKSQLYSN
TPSDFDFKLQ STARFLSQTA LKMLLKSVDL AFPVMHGQFG EDGGIQRLLE SYKVPYVGSG
VEACKRCSDK FDANTFIREQ GFFALPSQVL KIFHNDHGKR IRDFFKINKI KRAIVKPATG
GSSISVFSVG SPEEALEKAQ LIFSRRIDTR VVIEPFCEGV EFTVILLQNR FGMPVAVLPT
EMEMDYQNHQ IFDFRKKYLP TRQVTYHCPP RFDNETIERI QVQVEQLFTV LGMRDFARFD
GWLLPDGKLW FSDFNPISGM EQNSFLFQQS ARIGLSHRDV LRLIVKNACR RQGIPFPDFI
SKQKQKKKRK PVNVLFGGNT SERQVSLMSG TNVWLKLRQS ETYDPKPFLL DLNGEVWSVP
YALTLNHTVE EIYENCLRAK EDENRLRFLE EKVKLRLALE SEESSEDFVL PERMTLEQFL
NRSEFVFTGL HGGIGEDGTL QRMMVDANVK FNGPGEKASA LCMDKYATNQ ALKGLEAQGV
YVPNQRCIEL SELVSLKGKA FEKVWKELQG ELQARSVIVK PQSDGCSSGV VRLYSIADLK
QYVNWADKVA PFIPAGVFKN QVSMIEMPLT RMENLLFEPF IETDVVRVKG NQLKWRKKKG
WIEVTVGVVE RKGKMVALSP SLTVAEGEVL SLEEKFQGGT GINITPPSRD IVKPKALEKA
KKS
//
