ID A0A0G1CP18_9BACT Unreviewed; 341 AA.
AC A0A0G1CP18;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=D-alanine-D-alanine ligase-like protein {ECO:0000313|EMBL:KKS87299.1};
GN ORFNames=UV61_C0002G0020 {ECO:0000313|EMBL:KKS87299.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWB1_43_11.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618446 {ECO:0000313|EMBL:KKS87299.1, ECO:0000313|Proteomes:UP000034050};
RN [1] {ECO:0000313|EMBL:KKS87299.1, ECO:0000313|Proteomes:UP000034050}
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:KKS87299.1}.
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DR EMBL; LCFD01000002; KKS87299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1CP18; -.
DR STRING; 1618446.UV61_C0002G0020; -.
DR Proteomes; UP000034050; 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 GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; 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; IPR000291; D-Ala_lig_Van_CS.
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.
DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKS87299.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 114..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 341 AA; 38477 MW; 936E9919405B8344 CRC64;
MVIGLCFNVK TNAPSTDPTA QTDAEYDAPE TIAAIKAALI SGGHKVIEIE ADQECYLKLY
KLQNRLDIVF NIAEGMYGDA REAQVPIFCD ILEIPYTHSS ALTNAIKLDK ALTKKVLLYH
GIRTPEFQLF SRPNEPINSH FQYPLLLKPN AEGSSKGILN ANLVKNEKQL RERLRWLFKA
FSQPVLVEEF LPGREFTVAL LGNPPQTLPI IEQRLDRLPS NLQKFASYEV KWLWEDTLSD
PRIAYDCPAK LNPDLEKEIQ NISQDTFAAL NCRDVARVDI RLDKNGKPHV LEINTMPGLI
PGEDIISYFP IAARVAGYSY NSMLLAILEA ASKRYHLTKK H
//
