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Database: UniProt
Entry: R6N195_9FIRM
LinkDB: R6N195_9FIRM
Original site: R6N195_9FIRM 
ID   R6N195_9FIRM            Unreviewed;       228 AA.
AC   R6N195;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN   ORFNames=BN647_00468 {ECO:0000313|EMBL:CDC00096.1};
OS   Firmicutes bacterium CAG:41.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263021 {ECO:0000313|EMBL:CDC00096.1, ECO:0000313|Proteomes:UP000018139};
RN   [1] {ECO:0000313|EMBL:CDC00096.1, ECO:0000313|Proteomes:UP000018139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:41 {ECO:0000313|Proteomes:UP000018139};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC         from secreted and periplasmic proteins.; EC=3.4.21.89;
CC         Evidence={ECO:0000256|ARBA:ARBA00000677,
CC         ECO:0000256|RuleBase:RU003993};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004606,
CC       ECO:0000256|RuleBase:RU362042}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|RuleBase:RU362042}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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:CDC00096.1}.
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DR   EMBL; CBEM010000210; CDC00096.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6N195; -.
DR   Proteomes; UP000018139; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR   PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003993};
KW   Membrane {ECO:0000256|RuleBase:RU003993};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018139};
KW   Transmembrane {ECO:0000256|RuleBase:RU003993};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT   TRANSMEM        31..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003993"
FT   DOMAIN          28..219
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        59
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   228 AA;  25972 MW;  C0E0F306BFB30411 CRC64;
     MSEQEGKNEN VTKTTAKEDK KTSLAREIWE WVYTLAIAIV IAMLIKGFIF DIVRVDGSSM
     FPTLVDNDRL IVTKLGYTPK QGDIIILDSE YKNREEYFDR LAESKDKEEL SSFEKFFAQS
     SMPSNLKKKY YVKRIIAMPG QTIDLVDGKV YVDGEMLDEP YYDGLTTSID PTVEYPITVD
     DDCVFVMGDN RTRSKDSRSS ELGQVPFKAI LGKSQVRIWP LSDIGLTK
//
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