ID A0A0G9GNS0_LACPN Unreviewed; 370 AA.
AC A0A0G9GNS0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047};
DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
GN Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047,
GN ECO:0000313|EMBL:QHM48182.1};
GN ORFNames=ASV54_09615 {ECO:0000313|EMBL:APD01584.1}, AVR83_11005
GN {ECO:0000313|EMBL:AOB23449.1}, C7M40_00080
GN {ECO:0000313|EMBL:QHM48182.1}, LPJSA22_02173
GN {ECO:0000313|EMBL:ODO62168.1}, LpLQ80_10575
GN {ECO:0000313|EMBL:AWI40930.1};
OS Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1590 {ECO:0000313|EMBL:ODO62168.1, ECO:0000313|Proteomes:UP000094892};
RN [1] {ECO:0000313|Proteomes:UP000183026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF1298 {ECO:0000313|Proteomes:UP000183026};
RA McLeod A., Rud I., Axelsson L.;
RT "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT associated with unfavorable effect.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AOB23449.1, ECO:0000313|Proteomes:UP000093296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF {ECO:0000313|EMBL:AOB23449.1,
RC ECO:0000313|Proteomes:UP000093296};
RA Petkau K., Fast D., Duggal A., Foley E.;
RT "Comparative evaluation of the genomes of common bacterial members of the
RT Drosophila intestinal community.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ODO62168.1, ECO:0000313|Proteomes:UP000094892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSA22 {ECO:0000313|EMBL:ODO62168.1,
RC ECO:0000313|Proteomes:UP000094892};
RA Choi H.S.;
RT "Genome sequencing of Lactobacillus plantarum JSA22, isolated from
RT fermented soybean paste.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QHM48182.1, ECO:0000313|Proteomes:UP000465032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRCM101518 {ECO:0000313|EMBL:QHM48182.1,
RC ECO:0000313|Proteomes:UP000465032};
RA Jeong D.-Y.;
RT "Lactobacillus plantatrum SRCM101518 having antimicrbial activity species
RT isolated from Korea kimchi.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:AWI40930.1, ECO:0000313|Proteomes:UP000244922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LQ80 {ECO:0000313|EMBL:AWI40930.1,
RC ECO:0000313|Proteomes:UP000244922};
RA Moriya N., Nakano K., Shiroma A., Shinzato M., Ashimine N., Minami M.,
RA Tamotsu H., Shimoji M., Nakanishi T., Ohki S., Teruya K., Satou K.,
RA Hirano T., Hagi T., Kobayashi M., Nomura M., Kimoto H.N., Tajima K.,
RA Cai Y., Suzuki C.;
RT "Complete Genome Sequence of Lactobacillus plantarum Strain LQ80 Selected
RT for Preparation of Fermented Liquid Feed for Pig.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:APD01584.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MF1298 {ECO:0000313|EMBL:APD01584.1};
RA McLeod A., Fagerlund A., Rud I., Axelsson L.;
RT "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT associated with unfavorable effect.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
CC phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
CC ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00047};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR039102-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047}.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871, ECO:0000256|HAMAP-Rule:MF_00047}.
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DR EMBL; CP013753; AOB23449.1; -; Genomic_DNA.
DR EMBL; CP013149; APD01584.1; -; Genomic_DNA.
DR EMBL; CP028977; AWI40930.1; -; Genomic_DNA.
DR EMBL; MCOL01000001; ODO62168.1; -; Genomic_DNA.
DR EMBL; CP028241; QHM48182.1; -; Genomic_DNA.
DR RefSeq; WP_003644652.1; NZ_WYDR01000002.1.
DR GeneID; 77215726; -.
DR KEGG; lpb:SH83_10055; -.
DR PATRIC; fig|1590.142.peg.2161; -.
DR OMA; RVDFFYV; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000093296; Chromosome.
DR Proteomes; UP000094892; Unassembled WGS sequence.
DR Proteomes; UP000183026; Chromosome.
DR Proteomes; UP000244922; Chromosome.
DR Proteomes; UP000465032; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; 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 HAMAP; MF_00047; Dala_Dala_lig; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR000291; D-Ala_lig_Van_CS.
DR InterPro; IPR005905; D_ala_D_ala.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR011127; Dala_Dala_lig_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1.
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 Pfam; PF01820; Dala_Dala_lig_N; 1.
DR PIRSF; PIRSF039102; Ddl/VanB; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 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};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00047};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00047};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00047};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR039102-3};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR039102-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR039102-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00047}.
FT DOMAIN 142..348
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3"
SQ SEQUENCE 370 AA; 41347 MW; 28F5EB160958095B CRC64;
METQKKIHVG MLFGGNSSEH DVSKRSAHNI YDAMDKNKYE IDLFLITKNG IVLSDAATRR
VFDGEPEDQV VAEEMPKLDM SDPLAPIKNL TLAKDIDIFY PVVHGNLGED GTLQGLFKLL
KKPYVGSGVL ASAASFDKDI TKQILTHHHI QNTKYVVVTP ENRDQMTYAY LQAHVGDHLF
IKPANQGSSI GIHKAENEQE YLDGLADAFK YDYKILVEES IDNPREVECS ILGNENPKAS
KLGAIDVPKT DTFYDYNNKF VDASGVTFEL PVELPADLTK RIQQMSLDAF KALGLKGMAR
VDFLVSEDGE PYLGEINTLP GFTNISLYPK LWEVSGISYT ALIDQLIQLG FDEFKRQSDI
HYDFVALDAE
//
