EBSB_ENTFA
ID EBSB_ENTFA Reviewed; 135 AA.
AC P36921;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putative hydrolase EbsB {ECO:0000305};
DE EC=3.-.-.- {ECO:0000305};
GN Name=ebsB {ECO:0000303|PubMed:8226689}; OrderedLocusNames=EF_1728;
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], FUNCTION, AND SUBCELLULAR LOCATION.
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: Seems to play some role in the cell surface expression of a
CC chromosomally encoded receptor, named enterococcal binding substance
CC (EBS), that mediates mating aggregate formation. Might interfere with
CC the synthesis or assembly of EBS and function as a cell wall hydrolase.
CC {ECO:0000269|PubMed:8226689}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A7Y4};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305|PubMed:8226689}.
CC Note=Cell wall location was proposed in PubMed:8226689 based on a low
CC sequence similarity to a cell wall hydrolase and a penicillin-binding
CC protein. However, this protein has a best similarity to ribonucleases H
CC which are expected to be cytoplasmic. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase H family. EbsB subfamily.
CC {ECO:0000305}.
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DR EMBL; L23802; AAC36852.1; -; Unassigned_DNA.
DR EMBL; AE016830; AAO81503.1; -; Genomic_DNA.
DR PIR; B49939; B49939.
DR RefSeq; NP_815433.1; NC_004668.1.
DR RefSeq; WP_002369306.1; NZ_KE136528.1.
DR AlphaFoldDB; P36921; -.
DR SMR; P36921; -.
DR STRING; 226185.EF_1728; -.
DR EnsemblBacteria; AAO81503; AAO81503; EF_1728.
DR KEGG; efa:EF1728; -.
DR PATRIC; fig|226185.45.peg.1784; -.
DR eggNOG; COG0328; Bacteria.
DR HOGENOM; CLU_095977_2_1_9; -.
DR OMA; NTDHERW; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF13456; RVT_3; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 3: Inferred from homology;
KW Cell wall; Hydrolase; Magnesium; Metal-binding; Reference proteome;
KW Secreted.
FT CHAIN 1..135
FT /note="Putative hydrolase EbsB"
FT /id="PRO_0000195432"
FT DOMAIN 1..128
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A7Y4"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0A7Y4"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A7Y4"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A7Y4"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0A7Y4"
FT CONFLICT 55
FT /note="K -> Q (in Ref. 1; AAC36852)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="E -> K (in Ref. 1; AAC36852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 135 AA; 15371 MW; B03A7F80518862CD CRC64;
MLRIYVDAAT KGNPGESGGG IVYLTDQSRQ QLHVPLGIVS NHEAEFKVLI EALKKAIANE
DNQQTVLLHS DSKIVVQTIE KNYAKNEKYQ PYLAEYQQLE KNFPLLLIEW LPESQNKAAD
MLARQALQKF YPNKK
