ID A0A0N8PQX4_9CHLR Unreviewed; 206 AA.
AC A0A0N8PQX4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:KPV48333.1};
DE Flags: Fragment;
GN ORFNames=SE17_38620 {ECO:0000313|EMBL:KPV48333.1};
OS Kouleothrix aurantiaca.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Kouleothrix.
OX NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV48333.1, ECO:0000313|Proteomes:UP000050509};
RN [1] {ECO:0000313|EMBL:KPV48333.1, ECO:0000313|Proteomes:UP000050509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COM-B {ECO:0000313|EMBL:KPV48333.1,
RC ECO:0000313|Proteomes:UP000050509};
RA Hemp J.;
RT "Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPV48333.1}.
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DR EMBL; LJCR01002735; KPV48333.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8PQX4; -.
DR PATRIC; fig|186479.3.peg.5628; -.
DR Proteomes; UP000050509; 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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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 PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF25; D-ALANINE--D-ALANINE LIGASE A; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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 Ligase {ECO:0000313|EMBL:KPV48333.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000050509};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 5..198
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPV48333.1"
SQ SEQUENCE 206 AA; 22555 MW; 49AD2DC13278C423 CRC64;
PLLPWLLVQR ADWRKQPDAV AARVEAALQY PMFIKPANMG SSVGITKATD RATLAAGLDE
AARYDRRIVI EQGINAREIE ISVLGNDEVA ASVPGEVVPS KEWYDYEAKY LGGESQILIP
APIDAALAGQ VRELAIRAFK AIDGAGLARV DFLLDKDSGA LYLNEANTMP GFTSVSMYAK
MWDASGLTYN QLLDRLIELA LERNEE
//
