ID A0A0E8U2E5_MYCTX Unreviewed; 358 AA.
AC A0A0E8U2E5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=ddlA {ECO:0000313|EMBL:CKR60791.1};
GN Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047,
GN ECO:0000313|EMBL:OMH60925.1};
GN ORFNames=A4S10_03110 {ECO:0000313|EMBL:OMH60925.1}, ERS027659_01830
GN {ECO:0000313|EMBL:CKR60791.1}, ERS027661_02314
GN {ECO:0000313|EMBL:CKR91028.1}, ERS053720_03680
GN {ECO:0000313|EMBL:CFH96264.1}, SAMEA2683035_03539
GN {ECO:0000313|EMBL:SGI41762.1};
OS Mycobacterium tuberculosis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773 {ECO:0000313|EMBL:CKR60791.1, ECO:0000313|Proteomes:UP000050164};
RN [1] {ECO:0000313|Proteomes:UP000049023, ECO:0000313|Proteomes:UP000050164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2926STDY5723788 {ECO:0000313|EMBL:SGI41762.1,
RC ECO:0000313|Proteomes:UP000182946}, Bir 185
RC {ECO:0000313|EMBL:CKR60791.1, ECO:0000313|Proteomes:UP000050164}, and
RC Bir 187 {ECO:0000313|EMBL:CKR91028.1,
RC ECO:0000313|Proteomes:UP000049023};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CFH96264.1, ECO:0000313|Proteomes:UP000046674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0351H {ECO:0000313|EMBL:CFH96264.1,
RC ECO:0000313|Proteomes:UP000046674};
RG Pathogen Informatics;
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:OMH60925.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH60925.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M., Bigi F., Soria M.A.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:OMH60925.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH60925.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M.M., Lopez B., Blanco F.C., Sasiain M.C., De La Barrera S.,
RA Ritacco V., Bigi F., Soria M.A.;
RT "Protein polymorphisms may explain contrasting epidemiological fitness of
RT two variants of a multidrug-resistant Mycobacterium tuberculosis strain.";
RL Submitted (FEB-2017) 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; CFSW01000031; CFH96264.1; -; Genomic_DNA.
DR EMBL; CNFT01000375; CKR60791.1; -; Genomic_DNA.
DR EMBL; CNFU01000475; CKR91028.1; -; Genomic_DNA.
DR EMBL; LWDQ01000001; OMH60925.1; -; Genomic_DNA.
DR EMBL; FPTZ01000034; SGI41762.1; -; Genomic_DNA.
DR PATRIC; fig|1773.211.peg.3719; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000046674; Unassembled WGS sequence.
DR Proteomes; UP000049023; Unassembled WGS sequence.
DR Proteomes; UP000050164; Unassembled WGS sequence.
DR Proteomes; UP000182946; Unassembled WGS sequence.
DR Proteomes; UP000189452; 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 141..348
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 303
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 358 AA; 37929 MW; AD6E1F97738BE0D8 CRC64;
MFGGRSNEHA ISCVSAGSIL RNLDSRRFDV IAVGITPAGS WVLTDANPDA LTITNRELPQ
VKSGSGTELA LPADPRRGGQ LVSLPPGAGE VLESVDVVFP VLHGPYGEDG TIQGLLELAG
VPYVGAGVLA SAVGMDKEFT KKLLAADGLP VGAYAVLRPP RSTLHRQECE RLGLPVFVKP
ARGGSSIGVS RVSSWDQLPA AVARARRHDP KVIVEAAISG RELECGVLEM PDGTLEASTL
GEIRVAGVRG REDSFYDFAT KYLDDAAELD VPAKVDDQVA EAIRQLAIRA FAAIDCRGLA
RVDFFLTDDG PVINEINTMP GFTTISMYPR MWAASGVDYP TLLATMIETA LARGVGLH
//
