ID Q718G1_YEREN Unreviewed; 332 AA.
AC Q718G1;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN Name=lep {ECO:0000313|EMBL:AAQ11415.1};
GN Synonyms=lepB {ECO:0000313|EMBL:CFQ65048.1};
GN ORFNames=ERS137939_00124 {ECO:0000313|EMBL:CNE88867.1},
GN ERS137941_02463 {ECO:0000313|EMBL:CFQ65048.1}, I6I39_03070
GN {ECO:0000313|EMBL:QQU47751.1};
OS Yersinia enterocolitica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630 {ECO:0000313|EMBL:AAQ11415.1};
RN [1] {ECO:0000313|EMBL:AAQ11415.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCTC10460 {ECO:0000313|EMBL:AAQ11415.1};
RA Anastasov N., Scherer S.;
RT "Genetic analysis of the rnc operon of Yersinia enterocolitica.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CNE88867.1, ECO:0000313|Proteomes:UP000041356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP27818 {ECO:0000313|EMBL:CNE88867.1,
RC ECO:0000313|Proteomes:UP000041356};
RG Pathogen Informatics;
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CFQ65048.1, ECO:0000313|Proteomes:UP000048841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP26249 {ECO:0000313|EMBL:CFQ65048.1,
RC ECO:0000313|Proteomes:UP000048841};
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QQU47751.1, ECO:0000313|Proteomes:UP000595309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_1082 {ECO:0000313|EMBL:QQU47751.1,
RC ECO:0000313|Proteomes:UP000595309};
RA Blissenbach B., Krut O., Tallon L., Sadzewicz L., Zhao X., Boylan J.,
RA Ott S., Bowen H., Vavikolanu K., Mehta A., Aluvathingal J., Nadendla S.,
RA Yan Y., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (JAN-2021) 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: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362042}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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DR EMBL; AF542975; AAQ11415.1; -; Genomic_DNA.
DR EMBL; CGBR01000016; CFQ65048.1; -; Genomic_DNA.
DR EMBL; CPZF01000001; CNE88867.1; -; Genomic_DNA.
DR EMBL; CP068146; QQU47751.1; -; Genomic_DNA.
DR RefSeq; WP_005159411.1; NZ_UHIX01000001.1.
DR MEROPS; S26.001; -.
DR GeneID; 77328277; -.
DR KEGG; yef:FORC2_1032; -.
DR PATRIC; fig|630.128.peg.3323; -.
DR OMA; FKWAPAR; -.
DR Proteomes; UP000041356; Unassembled WGS sequence.
DR Proteomes; UP000048841; Unassembled WGS sequence.
DR Proteomes; UP000595309; Chromosome.
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; 2.170.230.10; -; 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 InterPro; IPR019766; Sign_pep_all-beta_subdom.
DR NCBIfam; TIGR02227; sigpep_I_bact; 2.
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, ECO:0000313|EMBL:CFQ65048.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993}.
FT DOMAIN 67..310
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 98
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 332 AA; 36413 MW; 1E6AC031252033A2 CRC64;
MANMFALILA IATLVTGIIW CFERFKWGPA RQAKIAAVNA QTAAIKAQTG SAVDNKTLAP
AAKQPGWIET CASVFPVLAL VFIVRSFIYE PFQIPSGSMM PTLLIGDFIL VEKFAYGIKD
PITQTTLIPT GHPKRGDIAV FKYPLDPRLD YIKRVVGLPG DRVSYNPISK EVTVQPACNT
GASCDSALPI TYSASEPSDF VQTFRYSGNG EASAGFFQIP LNQAVPDGGV RLRERTETLG
PVAHQILTVP GRQEQLGAYY QQPNQPLGVW VVPEGHYFMM GDNRDNSADS RYWGFVPERN
LVGKATAIWM SFEKQEGEWP TGVRLSRIGG IH
//
