ID A0A378C1A5_KLEPO Unreviewed; 97 AA.
AC A0A378C1A5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|ARBA:ARBA00012216};
DE EC=6.3.2.4 {ECO:0000256|ARBA:ARBA00012216};
GN Name=ddlB_1 {ECO:0000313|EMBL:STV58673.1};
GN ORFNames=NCTC5050_06614 {ECO:0000313|EMBL:STV58673.1};
OS Klebsiella pneumoniae subsp. ozaenae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
OC Klebsiella; Klebsiella pneumoniae complex.
OX NCBI_TaxID=574 {ECO:0000313|EMBL:STV58673.1, ECO:0000313|Proteomes:UP000255382};
RN [1] {ECO:0000313|EMBL:STV58673.1, ECO:0000313|Proteomes:UP000255382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5050 {ECO:0000313|EMBL:STV58673.1,
RC ECO:0000313|Proteomes:UP000255382};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. {ECO:0000256|ARBA:ARBA00003921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 D-alanine + ATP = D-alanyl-D-alanine + ADP + phosphate +
CC H(+); Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57416, ChEBI:CHEBI:57822,
CC ChEBI:CHEBI:456216; EC=6.3.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00047614};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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; UGLZ01000005; STV58673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A378C1A5; -.
DR Proteomes; UP000255382; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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: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 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:STV58673.1};
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:UP000255382}.
FT DOMAIN 32..94
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 97 AA; 10911 MW; 0FC5C32004D9BC68 CRC64;
MIMRRSISLM RRNISAQDLK IPRVSQLFRT WVLKAWNVLG CKGWGRIDVM LDSDGQFYLL
EANTSPGMTS HSLVPMAARQ AGMSFSQLVV RILDLAG
//
