ID A0A135IDS5_9GAMM Unreviewed; 388 AA.
AC A0A135IDS5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:KXF83494.1};
GN ORFNames=ATN88_16570 {ECO:0000313|EMBL:KXF83494.1};
OS Enterovibrio coralii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Enterovibrio.
OX NCBI_TaxID=294935 {ECO:0000313|EMBL:KXF83494.1, ECO:0000313|Proteomes:UP000070529};
RN [1] {ECO:0000313|EMBL:KXF83494.1, ECO:0000313|Proteomes:UP000070529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 912 {ECO:0000313|EMBL:KXF83494.1,
RC ECO:0000313|Proteomes:UP000070529};
RA Gomez-Gil B., Enciso-Ibarra J.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:KXF83494.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNTY01000004; KXF83494.1; -; Genomic_DNA.
DR RefSeq; WP_067409750.1; NZ_LNTY01000004.1.
DR AlphaFoldDB; A0A135IDS5; -.
DR STRING; 294935.ATN88_16570; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000070529; 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:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 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:KXF83494.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000070529}.
FT DOMAIN 132..356
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 388 AA; 43469 MW; D8D2CA1CD21158D6 CRC64;
MVAALFNPEQ MDWIKKRVKI AVICGGEKSC SKNYVYENLS PRSTKTYRTV AEDIVATLAQ
EGFDQLEVLE ESMHLPQQLK SQNVDMAFLN SGGLQGYDSM CHLPSMMEMC GVPYIGHTPM
TAGLLDNKLM LKNELSALGI PTAPFITLDQ GRTIHDASCQ RALDYIDQEF GEGYIVKPVV
GRASIHVYPV FDRSELQEVV ERVQSATNNV VLIEPYLSGA EFVAAVCGRV LYKESQLEEQ
EQPFVFSISQ RVLDEGEHIF TSMDVRPITA DRSRPVLDES LKADIADIVS RIFTAFNLQT
LIRVDLRMDN NGRLYVLEAN PKPDLKRPCG NQINLVTAGL AAEGMQYEEL LQSLIFNRLQ
YLYRNRPTTL AHCLSDSLFT LSQQGGRA
//
