ID LEP_STRR6 Reviewed; 204 AA.
AC P59662;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Signal peptidase I;
DE Short=SPase I;
DE EC=3.4.21.89;
DE AltName: Full=Leader peptidase I;
GN Name=lepB; Synonyms=spi; OrderedLocusNames=spr0364;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
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DR EMBL; AE007317; AAK99168.1; -; Genomic_DNA.
DR RefSeq; NP_357958.1; NC_003098.1.
DR RefSeq; WP_001048155.1; NC_003098.1.
DR AlphaFoldDB; P59662; -.
DR SMR; P59662; -.
DR STRING; 171101.spr0364; -.
DR MEROPS; S26.015; -.
DR GeneID; 66805594; -.
DR KEGG; spr:spr0364; -.
DR PATRIC; fig|171101.6.peg.405; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_5_0_9; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR CDD; cd06462; Peptidase_S24_S26; 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 Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..204
FT /note="Signal peptidase I"
FT /id="PRO_0000109534"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 38
FT /evidence="ECO:0000250"
FT ACT_SITE 76
FT /evidence="ECO:0000250"
SQ SEQUENCE 204 AA; 23498 MW; 3D56798C79C2C3CA CRC64;
MNLFKNFLKE WGLFLLILSL LALSRIFFWS NVRVEGHSMD PTLADGEILF VVKHLPIDRF
DIVVAHEEDG NKDIVKRVIG MPGDTIRYEN DKLYINDKET DEPYLADYIK RFKDDKLQST
YSGKGFEGNK GTFFRSIAQK AQAFTVDVNY NTNFSFTVPE GEYLLLGDDR LVSSDSRHVG
TFKAKDITGE AKFRFWPITR IGTF
//
