ID   AGRB_CLOPS              Reviewed;         214 AA.
AC   Q0SSQ8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Putative AgrB-like protein {ECO:0000255|HAMAP-Rule:MF_00784};
DE            EC=3.4.-.- {ECO:0000255|HAMAP-Rule:MF_00784};
GN   OrderedLocusNames=CPR_1532;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM101 / Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
CC   -!- FUNCTION: May be involved in the proteolytic processing of a quorum
CC       sensing system signal molecule precursor. {ECO:0000255|HAMAP-
CC       Rule:MF_00784}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00784};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00784}.
CC   -!- SIMILARITY: Belongs to the AgrB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00784}.
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DR   EMBL; CP000312; ABG86149.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SSQ8; -.
DR   SMR; Q0SSQ8; -.
DR   EnsemblBacteria; ABG86149; ABG86149; CPR_1532.
DR   KEGG; cpr:CPR_1532; -.
DR   OMA; GAHFNTP; -.
DR   BioCyc; CPER289380:GI76-1544-MON; -.
DR   Proteomes; UP000001824; 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   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF04647; AgrB; 1.
DR   SMART; SM00793; AgrB; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Quorum sensing;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..214
FT                   /note="Putative AgrB-like protein"
FT                   /id="PRO_1000046836"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00784"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00784"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00784"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00784"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00784"
SQ   SEQUENCE   214 AA;  24255 MW;  786F686CA56BCCD1 CRC64;
     MIENLSKLIS EKVSSELNYD NERKEIIQYG TYALIQTLIS IISVFIIGLL FNIALEALIF
     LFTASILRKY SGGAHSESSN VCTLLGIIIS ICIGFLVKSS FFTKMNFEII VFIGIVIFVF
     GYFIVFKFAP VDTKNKPIKT EKKKKRMKKG SLKILTIYLF IEILSIILYY NLGWSLVKSV
     MLSIILGVAW QCITLTYIGN ILLKTIDSFT NKLL