VANL_STRCO
ID VANL_STRCO Reviewed; 346 AA.
AC Q9XAK7;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative D-alanine--D-lactate ligase;
DE EC=6.3.2.-;
DE AltName: Full=Vancomycin resistance-like protein;
GN OrderedLocusNames=SCO3595; ORFNames=SC66T3.06;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Required for resistance to glycopeptides antibiotics. D-Ala--
CC D-Ala ligase of altered specificity which catalyzes ester bond
CC formation between D-Ala and various D-hydroxy acids; producing a
CC peptidoglycan which does not terminate by D-alanine but by D-lactate,
CC thus preventing vancomycin binding (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- MISCELLANEOUS: S.coelicolor was found to be of intermediate resistance
CC to vancomycin although it does not produce vancomycin.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000305}.
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DR EMBL; AL939117; CAB45462.1; -; Genomic_DNA.
DR PIR; T35363; T35363.
DR RefSeq; NP_627790.1; NC_003888.3.
DR RefSeq; WP_011029110.1; NZ_VNID01000003.1.
DR AlphaFoldDB; Q9XAK7; -.
DR SMR; Q9XAK7; -.
DR STRING; 100226.SCO3595; -.
DR GeneID; 1099031; -.
DR KEGG; sco:SCO3595; -.
DR PATRIC; fig|100226.15.peg.3652; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_0_0_11; -.
DR InParanoid; Q9XAK7; -.
DR OMA; IPYVGCD; -.
DR PhylomeDB; Q9XAK7; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 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 Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01820; Dala_Dala_lig_N; 1.
DR PIRSF; PIRSF039102; Ddl/VanB; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 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 Antibiotic resistance; ATP-binding; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Ligase; Magnesium; Manganese; Membrane;
KW Metal-binding; Nucleotide-binding; Peptidoglycan synthesis;
KW Reference proteome.
FT CHAIN 1..346
FT /note="Putative D-alanine--D-lactate ligase"
FT /id="PRO_0000177920"
FT DOMAIN 137..338
FT /note="ATP-grasp"
FT BINDING 163..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 37295 MW; 0BD20328A038A4FA CRC64;
MARLKVGIVF GGSSEEHAVS VKSAQEVARN LDTEKYQPFF VGITKDGAWR LCDGPGQDWE
NGDCRPVVLS PDRSVHGLLV LEQGQYRSVR LDVVLPVLHG TLGEDGATQG LLELSGIPYV
GCDVQSSALC MDKSLAYVVA RSAGIATPDF WTVTGDETID PGRLTYPVFV KPARSGSSFG
VSKVCRPEDL ATAVESARRY DTKVLIEAAV VGSEVGCAIL GNDPDLIVGE VDRIALSHGF
FRIHQEEQPE NGSENSTPVV PADIPTEKRS LVQETAKAVY RALGCRGLSR VDMFLKEDGE
VVLNEVNTLP GMTSYSRYPR MMAAAGLPLS EVIDRTLSLA LTGKLR
