ID   FSRB_ENTFA              Reviewed;         242 AA.
AC   P0DH69; Q833V5; Q9RQG4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Protein FsrB;
DE   AltName: Full=AgrBfs;
GN   Name=fsrB; OrderedLocusNames=EF_1821;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
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: May be involved in the proteolytic processing of a quorum
CC       sensing system signal molecule precursor required for the regulation of
CC       the virulence genes for gelatinase (gelE) and a serine protease (sprE).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AgrB family. {ECO:0000305}.
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DR   EMBL; AE016830; AAO81588.1; -; Genomic_DNA.
DR   RefSeq; NP_815518.1; NC_004668.1.
DR   RefSeq; WP_002369249.1; NZ_KE136528.1.
DR   AlphaFoldDB; P0DH69; -.
DR   STRING; 226185.EF_1821; -.
DR   MEROPS; C75.002; -.
DR   EnsemblBacteria; AAO81588; AAO81588; EF_1821.
DR   KEGG; efa:EF1821; -.
DR   PATRIC; fig|226185.45.peg.1699; -.
DR   eggNOG; COG4512; Bacteria.
DR   HOGENOM; CLU_1145793_0_0_9; -.
DR   OMA; MKFAIVY; -.
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   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00784; AgrB; 1.
DR   InterPro; IPR006741; AgrB.
DR   Pfam; PF04647; AgrB; 1.
DR   SMART; SM00793; AgrB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Quorum sensing;
KW   Reference proteome; Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..242
FT                   /note="Protein FsrB"
FT                   /id="PRO_0000168133"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   242 AA;  27613 MW;  CEB26B6BFFBF3EBD CRC64;
     MLIDWILKNI MDMDQEDQSG KTQWTKYYLT VYFSGLFNLL MILILSVLFG TLSETFIVYV
     VLIFLRPVAG GWHAKTKWLC RLESIVIYVA IPFVLKNSSV SLPFIYKILL MCLLVVLFYW
     YAPQGTAIEP VQPSDLNVLK KQSLIRVCLL ILCSLFVKEK IASVILYGLV IQGLMILPVT
     KNLIEGSVFM KFGKKIIKNV IEKRVAKVSD GVGTKPRLNQ NSPNIFGQWM GQTEKPKKNI
     EK