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Database: UniProt
Entry: A0A0S4LD55_9BACT
LinkDB: A0A0S4LD55_9BACT
Original site: A0A0S4LD55_9BACT 
ID   A0A0S4LD55_9BACT        Unreviewed;       340 AA.
AC   A0A0S4LD55;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=D-alanine-D-alanine ligase {ECO:0000313|EMBL:CUS33846.1};
DE            EC=6.3.2.4 {ECO:0000313|EMBL:CUS33846.1};
GN   Name=ddlA {ECO:0000313|EMBL:CUS33846.1};
GN   ORFNames=COMA1_11372 {ECO:0000313|EMBL:CUS33846.1};
OS   Candidatus Nitrospira nitrosa.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Nitrospira.
OX   NCBI_TaxID=1742972 {ECO:0000313|EMBL:CUS33846.1, ECO:0000313|Proteomes:UP000199032};
RN   [1] {ECO:0000313|EMBL:CUS33846.1, ECO:0000313|Proteomes:UP000199032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COMA1 {ECO:0000313|EMBL:CUS33846.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CZQA01000001; CUS33846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4LD55; -.
DR   STRING; 1742972.COMA1_11372; -.
DR   OrthoDB; 9813261at2; -.
DR   Proteomes; UP000199032; 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:UniProtKB-EC.
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:CUS33846.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199032}.
FT   DOMAIN          117..329
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   340 AA;  38408 MW;  207BE6E6ED6B71A5 CRC64;
     MKRLRVLVLM HEDLVPPEQV SGHDLQSVAW RTEYDVVTTL KKLGHDVYPL GVKSDLSVIQ
     AAIDQWKPDI AFNLLEEFDG VAVYDQHVVS YLELLHMPYT GCNPRGLMLA RDKVLTKKVL
     AFHRIPYPDF MDVPQGRVAK RPKQLTFPLI VKSVSEEASL GISQASIVED DDKLSERVAF
     IHNSVGSGAL VERYIEGREL YVGIIGNGHL QVLPVWELIM DKLPEDAKRI ATERVKWSPK
     YQEKYGITSR EAAHLPDGKA QEIQDLTKRV YRALGLSGYA RIDMRMDAEG QLYVLEANPN
     PQIAEDEDFA DSAKETGYAY TELLQELLNV GLRWRPAKAA
//
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