ID C4ID34_CLOBU Unreviewed; 188 AA.
AC C4ID34;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 Name=lepB_1 {ECO:0000313|EMBL:EEP55803.1};
GN ORFNames=CLP_3263 {ECO:0000313|EMBL:EEP55803.1};
OS Clostridium butyricum E4 str. BoNT E BL5262.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP55803.1, ECO:0000313|Proteomes:UP000003081};
RN [1] {ECO:0000313|EMBL:EEP55803.1, ECO:0000313|Proteomes:UP000003081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.;
RL Submitted (AUG-2009) 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:EEP55803.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACOM01000002; EEP55803.1; -; Genomic_DNA.
DR RefSeq; WP_003413763.1; NZ_ACOM01000002.1.
DR AlphaFoldDB; C4ID34; -.
DR STRING; 1492.ATN24_16740; -.
DR GeneID; 66380293; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_5_1_9; -.
DR Proteomes; UP000003081; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003993, ECO:0000313|EMBL:EEP55803.1};
KW Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Reference proteome {ECO:0000313|Proteomes:UP000003081};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 29..53
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 27..179
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 57
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 98
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 188 AA; 21491 MW; 2E4BDE4F10DD9921 CRC64;
MKENDIIENK EIENDGESKE KKGNFFKDWI IPILCAIAIA VAINKFVFIN VYIPSGSMIP
TLNINDKLIV TRIWNKDSIK RGDIIVFKSE ELNETVIKRV IGLPGDHVEI TDGLVKVNGE
QIDESYVKNN ESYNGIFDVP EGKLLFLGDN RAVSYDARYW ENPYIDEDDV QGKAQLRYYP
ISDFGLVR
//
