VANB_ENTFA
ID VANB_ENTFA Reviewed; 342 AA.
AC Q06893; Q47821; Q57112;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Vancomycin B-type resistance protein VanB;
DE EC=6.1.2.1;
DE AltName: Full=D-alanine--D-lactate ligase;
DE AltName: Full=VanB ligase;
GN Name=vanB; Synonyms=vanB2; OrderedLocusNames=EF_2294;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC STRAIN=ATCC 700802 / V583;
RX PubMed=8125347; DOI=10.1016/0378-1119(94)90737-4;
RA Evers S., Reynolds P.E., Courvalin P.;
RT "Sequence of the vanB and ddl genes encoding D-alanine:D-lactate and D-
RT alanine:D-alanine ligases in vancomycin-resistant Enterococcus faecalis
RT V583.";
RL Gene 140:97-102(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=8631706; DOI=10.1128/jb.178.5.1302-1309.1996;
RA Evers S., Courvalin P.;
RT "Regulation of VanB-type vancomycin resistance gene expression by the
RT VanS(B)-VanR(B) two-component regulatory system in Enterococcus faecalis
RT V583.";
RL J. Bacteriol. 178:1302-1309(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [4]
RP PROTEIN SEQUENCE OF 1-11, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700802 / V583;
RX PubMed=7957913; DOI=10.1016/0014-5793(94)01096-x;
RA Meziane-Cherif D., Badet-Denisot M.A., Evers S., Courvalin P., Badet B.;
RT "Purification and characterization of the VanB ligase associated with type
RT B vancomycin resistance in Enterococcus faecalis V583.";
RL FEBS Lett. 354:140-142(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-305.
RC STRAIN=ATCC 700802 / V583;
RX PubMed=8440477; DOI=10.1016/0378-1119(93)90779-3;
RA Evers S., Sahm D.F., Courvalin P.;
RT "The vanB gene of vancomycin-resistant Enterococcus faecalis V583 is
RT structurally related to genes encoding D-Ala:D-Ala ligases and
RT glycopeptide-resistance proteins VanA and VanC.";
RL Gene 124:143-144(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-312.
RC STRAIN=SF300;
RX PubMed=8215270; DOI=10.1128/aac.37.8.1604;
RA Gold H.S., Uenal S., Cercenado E., Thauvin-Eliopoulos C., Eliopoulos G.M.,
RA Wennersten C.B., Moellering R.C. Jr.;
RT "A gene conferring resistance to vancomycin but not teicoplanin in isolates
RT of Enterococcus faecalis and Enterococcus faecium demonstrates homology
RT with vanB, vanA, and vanC genes of enterococci.";
RL Antimicrob. Agents Chemother. 37:1604-1609(1993).
CC -!- FUNCTION: Required for high-level resistance to glycopeptides
CC antibiotics. D-Ala--D-Ala ligase of altered specificity which catalyzes
CC ester bond formation between D-Ala and various D-hydroxy acids;
CC producing a peptidoglycan which does not terminate in D-alanine but in
CC D-lactate, thus preventing vancomycin binding.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lactate + ATP + D-alanine = ADP + D-alanyl-(R)-lactate +
CC phosphate; Xref=Rhea:RHEA:37347, ChEBI:CHEBI:16004,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
CC ChEBI:CHEBI:61166, ChEBI:CHEBI:456216; EC=6.1.2.1;
CC Evidence={ECO:0000269|PubMed:7957913};
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; Peripheral membrane protein;
CC Cytoplasmic side.
CC -!- INDUCTION: By vancomycin.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000305}.
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DR EMBL; U00456; AAC43217.1; -; Unassigned_DNA.
DR EMBL; U35369; AAB05627.1; -; Genomic_DNA.
DR EMBL; AE016830; AAO82021.1; -; Genomic_DNA.
DR EMBL; L06138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L15304; AAA24785.1; -; Genomic_DNA.
DR PIR; PN0478; PN0478.
DR RefSeq; NP_815951.1; NC_004668.1.
DR RefSeq; WP_002368691.1; NZ_KE136528.1.
DR AlphaFoldDB; Q06893; -.
DR SMR; Q06893; -.
DR STRING; 226185.EF_2294; -.
DR EnsemblBacteria; AAO82021; AAO82021; EF_2294.
DR KEGG; efa:EF2294; -.
DR PATRIC; fig|226185.45.peg.1238; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_0_0_9; -.
DR OMA; IPYVGCD; -.
DR BioCyc; MetaCyc:MON-15464; -.
DR SABIO-RK; Q06893; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
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; 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 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 1: Evidence at protein level;
KW Antibiotic resistance; ATP-binding; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Direct protein sequencing; Ligase;
KW Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..342
FT /note="Vancomycin B-type resistance protein VanB"
FT /id="PRO_0000177918"
FT DOMAIN 136..337
FT /note="ATP-grasp"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 168..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 176..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 303..304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VARIANT 106
FT /note="A -> C (in strain: SF300)"
FT VARIANT 153
FT /note="E -> D (in strain: SF300)"
FT VARIANT 161..162
FT /note="RT -> GA (in strain: SF300)"
FT VARIANT 185
FT /note="S -> G (in strain: SF300)"
FT VARIANT 258
FT /note="I -> T (in strain: SF300)"
SQ SEQUENCE 342 AA; 37332 MW; AA109AB455672449 CRC64;
MNKIKVAIIF GGCSEEHDVS VKSAIEIAAN INTEKFDPHY IGITKNGVWK LCKKPCTEWE
ADSLPAIFSP DRKTHGLLVM KEREYETRRI DVAFPVLHGK CGEDGAIQGL FELSGIPYVG
CDIQSSAACM DKSLAYILTK NAGIAVPEFQ MIEKGDKPEA RTLTYPVFVK PARSGSSFGV
TKVNSTEELN AAIEAAGQYD GKILIEQAIS GCEVGCAVMG NEDDLIVGEV DQIRLSHGIF
RIHQENEPEK GSENAMIIVP ADIPVEERNR VQETAKKVYR VLGCRGLARV DLFLQEDGGI
VLNEVNTLPG FTSYSRYPRM AAAAGITLPA LIDSLITLAI ER
