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Database: UniProt
Entry: E0MYP0_9CORY
LinkDB: E0MYP0_9CORY
Original site: E0MYP0_9CORY 
ID   E0MYP0_9CORY            Unreviewed;       254 AA.
AC   E0MYP0;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 50.
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   Name=lepB {ECO:0000313|EMBL:EFM43336.1};
GN   ORFNames=HMPREF0277_1624 {ECO:0000313|EMBL:EFM43336.1};
OS   Corynebacterium accolens ATCC 49726.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=862512 {ECO:0000313|EMBL:EFM43336.1, ECO:0000313|Proteomes:UP000004599};
RN   [1] {ECO:0000313|EMBL:EFM43336.1, ECO:0000313|Proteomes:UP000004599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49726 {ECO:0000313|EMBL:EFM43336.1,
RC   ECO:0000313|Proteomes:UP000004599};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUL-2010) 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: Membrane {ECO:0000256|RuleBase:RU362042}; Single-
CC       pass type II membrane protein {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:EFM43336.1}.
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DR   EMBL; AEED01000114; EFM43336.1; -; Genomic_DNA.
DR   RefSeq; WP_005278658.1; NZ_GL397138.1.
DR   AlphaFoldDB; E0MYP0; -.
DR   HOGENOM; CLU_028723_0_0_11; -.
DR   Proteomes; UP000004599; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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; 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; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:EFM43336.1};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU362042};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        26..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          27..239
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   254 AA;  27696 MW;  B06EE18B7CBAF6E8 CRC64;
     MNNESISQGK EAAAEEATTE KKQMPWWLET LVVVVSVLVV VGLFQNFIGR QYVIPSGSME
     PTLHGCEGCT NDRIFTEKVS YYGDKSPEPG DVVVFKGTDD WNGSYVSPRS SNAVIHGIQD
     ALSFISLAPP DENTLVKRVI ATGGQTVSCQ EGDPAVMVDG KPIKQDYVQD PPTYPVDEST
     GSEACGGPYF GPVKVPEDNI WVMGDNRTAS ADSRYHMGDN FHGTIPVDNV RGKVQFVFWP
     FNRIGGVDDP DIQS
//
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