ID   R5RJN9_9FIRM            Unreviewed;       153 AA.
AC   R5RJN9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Signal peptidase II {ECO:0000313|EMBL:CCZ34986.1};
GN   ORFNames=BN747_00521 {ECO:0000313|EMBL:CCZ34986.1};
OS   Firmicutes bacterium CAG:646.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262995 {ECO:0000313|EMBL:CCZ34986.1, ECO:0000313|Proteomes:UP000018386};
RN   [1] {ECO:0000313|EMBL:CCZ34986.1, ECO:0000313|Proteomes:UP000018386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:646 {ECO:0000313|Proteomes:UP000018386};
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:CCZ34986.1}.
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DR   EMBL; CAZW010000150; CCZ34986.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5RJN9; -.
DR   STRING; 1262995.BN747_00521; -.
DR   Proteomes; UP000018386; 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:UP000018386};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        127..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   153 AA;  16907 MW;  691280C8639A4353 CRC64;
     MVWLSVAAAI FFADSGIKHW AEKKLSDKAV REVAGDRILL RRLHNSGMAC SVGEKHPQAV
     KVGTLTLWGI CFLGFCRLLK LPGKKLEKAA GACILGGGAS NMADRLTRGY VVDYFSFNVK
     WEKLRRLVFN ISDLFILGGT LLSLVGLLKR KDR
//