ID   R7N5E7_9FIRM            Unreviewed;       156 AA.
AC   R7N5E7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CDF07801.1};
GN   ORFNames=BN816_02490 {ECO:0000313|EMBL:CDF07801.1};
OS   Firmicutes bacterium CAG:95.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262988 {ECO:0000313|EMBL:CDF07801.1, ECO:0000313|Proteomes:UP000018182};
RN   [1] {ECO:0000313|EMBL:CDF07801.1, ECO:0000313|Proteomes:UP000018182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:95 {ECO:0000313|Proteomes:UP000018182};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A8 family.
CC       {ECO:0000256|ARBA:ARBA00006139, ECO:0000256|RuleBase:RU004181}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDF07801.1}.
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DR   EMBL; CBKF010000162; CDF07801.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7N5E7; -.
DR   STRING; 1262988.BN816_02490; -.
DR   Proteomes; UP000018182; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001872; Peptidase_A8.
DR   PANTHER; PTHR33695; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR   PANTHER; PTHR33695:SF1; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018182};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   156 AA;  17617 MW;  BBE49B7765E61180 CRC64;
     MKRPVGKLFV HLFAITGIAG TDLYIKKQIE EKKEMNCCEP ICRGKLLLRR YHNRGAFLNL
     GEKNPQLVAA ISVGMTVFAL LLFISTFSFL GKGMLRWGLT MLLGGAFSNT YDRLKRKYVV
     DYVSFNVPWE AFRKIVFNIG DFAIMIGALV SVLSEV
//