ID   EBSA_ENTFA              Reviewed;         153 AA.
AC   P36920;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Protein EbsA {ECO:0000305};
GN   Name=ebsA {ECO:0000303|PubMed:8226689}; OrderedLocusNames=EF_1727;
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 FUNCTION.
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/or assist in the localization of
CC       EbsB to the cell wall. {ECO:0000269|PubMed:8226689}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the EbsA family. {ECO:0000305}.
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DR   EMBL; L23802; AAC36851.1; -; Unassigned_DNA.
DR   EMBL; AE016830; AAO81502.1; -; Genomic_DNA.
DR   PIR; A49939; A49939.
DR   RefSeq; NP_815432.1; NC_004668.1.
DR   RefSeq; WP_002357403.1; NZ_KE136528.1.
DR   AlphaFoldDB; P36920; -.
DR   STRING; 226185.EF_1727; -.
DR   EnsemblBacteria; AAO81502; AAO81502; EF_1727.
DR   GeneID; 60894023; -.
DR   KEGG; efa:EF1727; -.
DR   PATRIC; fig|226185.45.peg.1785; -.
DR   eggNOG; ENOG50349T2; Bacteria.
DR   HOGENOM; CLU_135677_1_0_9; -.
DR   OMA; HFKGEVE; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR020215; EbsA-like.
DR   Pfam; PF17255; EbsA; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..153
FT                   /note="Protein EbsA"
FT                   /id="PRO_0000086908"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        118..119
FT                   /note="IP -> DS (in Ref. 1; AAC36851)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="V -> I (in Ref. 1; AAC36851)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   153 AA;  17837 MW;  4D2608413406F689 CRC64;
     MKKQKFYWQP ELASTIIYWS CTFCILFISL ILALENNGPY LISNLVMVPF FVFAYLGIAR
     SFNMTETSLI VRDVLWFRKK ALPLSQIEKV TYNEKSIEIF SSEFKEGSKV FLMKKKTIPL
     FLEALKVKKP ELKVAEDHSL GLHKKEEKNK SES