EBSC_ENTFA
ID EBSC_ENTFA Reviewed; 164 AA.
AC P36922;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Putative Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase EbsC;
DE EC=4.2.-.-;
DE AltName: Full=Protein EbsC;
GN OrderedLocusNames=EF_1730;
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].
RC STRAIN=OG1SSP;
RX PubMed=8226689; DOI=10.1128/jb.175.22.7421-7429.1993;
RA Bensing B.A., Dunny G.M.;
RT "Cloning and molecular analysis of genes affecting expression of binding
RT substance, the recipient-encoded receptor(s) mediating mating aggregate
RT formation in Enterococcus faecalis.";
RL J. Bacteriol. 175:7421-7429(1993).
RN [2]
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).
CC -!- FUNCTION: Affects the expression of the receptor, named binding
CC substance, that mediates mating aggregate formation. Could be a
CC regulatory protein that suppresses the function or expression of ebsA
CC and/or ebsMB.
CC -!- SIMILARITY: Belongs to the prolyl-tRNA editing family. YbaK/EbsC
CC subfamily. {ECO:0000305}.
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DR EMBL; L23802; AAC36853.1; -; Unassigned_DNA.
DR EMBL; AE016830; AAO81504.1; -; Genomic_DNA.
DR PIR; C49939; C49939.
DR RefSeq; NP_815434.1; NC_004668.1.
DR RefSeq; WP_002357401.1; NZ_KE136528.1.
DR AlphaFoldDB; P36922; -.
DR SMR; P36922; -.
DR STRING; 226185.EF_1730; -.
DR EnsemblBacteria; AAO81504; AAO81504; EF_1730.
DR KEGG; efa:EF1730; -.
DR PATRIC; fig|226185.45.peg.1783; -.
DR eggNOG; COG2606; Bacteria.
DR HOGENOM; CLU_094875_3_0_9; -.
DR OMA; PYDYVEH; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd00002; YbaK_deacylase; 1.
DR Gene3D; 3.90.960.10; -; 1.
DR InterPro; IPR004369; Prolyl-tRNA_editing_YbaK/EbsC.
DR InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR Pfam; PF04073; tRNA_edit; 1.
DR PIRSF; PIRSF006181; EbsC_YbaK; 1.
DR SUPFAM; SSF55826; SSF55826; 1.
DR TIGRFAMs; TIGR00011; YbaK_EbsC; 1.
PE 3: Inferred from homology;
KW Lyase; Protein biosynthesis; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..164
FT /note="Putative Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase EbsC"
FT /id="PRO_0000086909"
FT CONFLICT 111
FT /note="I -> T (in Ref. 1; AAC36853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 164 AA; 18057 MW; 6EB3FD4CA5853B89 CRC64;
MAKKKTQQKT NAMRMVEQHK VPYKEYEFAW SEDHLSAESV AESLGIEKGR IFKTLVTVGN
KTGPVVAVIP GNQELDLKKL AKASGNKKVE MLHLKDLEAT TGYIRGGCSP IGMKKQFPTY
LAEEAQQYSA IIVSAGKRGM QIELAPEAIL SLTNGQFAEI TTKE