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Database: UniProt
Entry: S1RN35_9ENTE
LinkDB: S1RN35_9ENTE
Original site: S1RN35_9ENTE 
ID   S1RN35_9ENTE            Unreviewed;       181 AA.
AC   S1RN35;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN   ORFNames=OMO_00261 {ECO:0000313|EMBL:ESK62612.1};
OS   Enterococcus cecorum DSM 20682 = ATCC 43198.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1121864 {ECO:0000313|EMBL:ESK62612.1, ECO:0000313|Proteomes:UP000017415};
RN   [1] {ECO:0000313|EMBL:ESK62612.1, ECO:0000313|Proteomes:UP000017415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43198 {ECO:0000313|EMBL:ESK62612.1,
RC   ECO:0000313|Proteomes:UP000017415};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus cecorum DSM 20682 (= ATCC 43198)
RT   (Illumina assembly).";
RL   Submitted (OCT-2013) 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:RU362042};
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|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:ESK62612.1}.
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DR   EMBL; AHYS01000001; ESK62612.1; -; Genomic_DNA.
DR   RefSeq; WP_016251933.1; NZ_KI535313.1.
DR   AlphaFoldDB; S1RN35; -.
DR   STRING; 44008.GCA_001318175_00624; -.
DR   GeneID; 60871426; -.
DR   PATRIC; fig|1121864.4.peg.1796; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_5_0_9; -.
DR   OrthoDB; 9802919at2; -.
DR   Proteomes; UP000017415; 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; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR   PANTHER; PTHR43390:SF8; SIGNAL PEPTIDASE I; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 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:RU362042};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017415};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          13..172
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        41
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   181 AA;  20982 MW;  78F03AF8E494C57A CRC64;
     MIPTKYLDSF WLLVKYLLIS LGIALVLRGF IFIPMMVEGN SMNPLLDNRD MILVERLTKI
     KRFDVIVFQE GGTTYIKRVI ALPGEKLAYK KQQLYINDKP VKEYFKDSHL SKKEQSLYYD
     MNDFSLDDLL GVEKLGRDSY FVLGDNRRIS KDSRSFGTVS SEQILGKACG IYYPFTHIKI
     I
//
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