ID   A0A2N8ZJX3_9VIBR        Unreviewed;       384 AA.
AC   A0A2N8ZJX3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=D-ala D-ala ligase {ECO:0000313|EMBL:SON52176.1};
GN   ORFNames=VTAP4600_B0565 {ECO:0000313|EMBL:SON52176.1};
OS   Vibrio tapetis subsp. tapetis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1671868 {ECO:0000313|EMBL:SON52176.1, ECO:0000313|Proteomes:UP000235828};
RN   [1] {ECO:0000313|EMBL:SON52176.1, ECO:0000313|Proteomes:UP000235828}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vibrio tapetis CECT4600 {ECO:0000313|EMBL:SON52176.1};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) 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}.
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DR   EMBL; LT960612; SON52176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N8ZJX3; -.
DR   KEGG; vta:B0565; -.
DR   OrthoDB; 9813261at2; -.
DR   Proteomes; UP000235828; Chromosome b.
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:SON52176.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235828}.
FT   DOMAIN          132..356
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   384 AA;  42861 MW;  CBCD6AE2F40FB609 CRC64;
     MTNFIFSPAQ LNWIRNKLKI AVIHGGDKAQ PRGFIFENLS PRSTKTYEAV AHDIANALRE
     SGFQLVTVLA EDIYLAETLR QEQVDLVITN SGGLQGFDSM CHLPSMLEML GVPYVGHSPM
     TAGLLDNKHL FKHEIKAAGL PTAPFITIGI DEDFASESNQ RALDDIARRF PQGFIVKPVS
     GRASIHVYPV FDRSELASTV EKVRQASNNI VMIEPFLGGR EFVVAVAGEY TFKQGELTQS
     DKPMAFSITE RVLGADEPIF TSMDIKPITQ DRLIAVTEQP LRDQLAEIGQ KIYRQLGLQT
     LVRVDMRMDN AGNLYVLETN PKPDLKRPEG DKVSLVCHDL QREGMSYTDL IQSLVFNRLS
     FLKAKRPMAL AHCLNEQFDL IGDV
//