ID Q706G3_STRMT Unreviewed; 157 AA.
AC Q706G3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
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};
DE Flags: Fragment;
GN Name=spi {ECO:0000313|EMBL:CAF02030.1};
OS Streptococcus mitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=28037 {ECO:0000313|EMBL:CAF02030.1};
RN [1] {ECO:0000313|EMBL:CAF02030.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B6 {ECO:0000313|EMBL:CAF02030.1}, and HER 1055
RC {ECO:0000313|EMBL:CAF02021.1};
RX PubMed=15576771; DOI=10.1128/JB.186.24.8229-8239.2004;
RA Romero P., Lopez R., Garcia E.;
RT "Characterization of LytA-like N-acetylmuramoyl-L-alanine amidases from two
RT new Streptococcus mitis bacteriophages provides insights into the
RT properties of the major pneumococcal autolysin.";
RL J. Bacteriol. 186:8229-8239(2004).
RN [2] {ECO:0000313|EMBL:ABG56207.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2859 {ECO:0000313|EMBL:ABG56207.1};
RX PubMed=16971639; DOI=10.1128/JCM.01137-06;
RA Balsalobre L., Hernandez-Madrid A., Llull D., Martin-Galiano A.J.,
RA Garcia E., Fenoll A., de la Campa A.G.;
RT "Molecular characterization of disease-associated streptococci of the mitis
RT group that are optochin susceptible.";
RL J. Clin. Microbiol. 44:4163-4171(2006).
RN [3] {ECO:0000313|EMBL:ABU53200.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B5 {ECO:0000313|EMBL:ABU53234.1}, HUO8
RC {ECO:0000313|EMBL:ABU53200.1}, Rsa42 {ECO:0000313|EMBL:ABU53209.1},
RC Rsa60 {ECO:0000313|EMBL:ABU53210.1}, S578
RC {ECO:0000313|EMBL:ABU53231.1}, S661 {ECO:0000313|EMBL:ABU53229.1},
RC SV16 {ECO:0000313|EMBL:ABU53233.1}, and SV5
RC {ECO:0000313|EMBL:ABU53224.1};
RX PubMed=17459765; DOI=10.1016/j.ijmm.2007.02.009;
RA Chi F., Nolte O., Bergmann C., Ip M., Hakenbeck R.;
RT "Crossing the barrier: evolution and spread of a major class of mosaic
RT pbp2x in Streptococcus pneumoniae, S. mitis and S. oralis.";
RL Int. J. Med. Microbiol. 297:503-512(2007).
RN [4] {ECO:0000313|EMBL:ABU53200.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B5 {ECO:0000313|EMBL:ABU53234.1}, HUO8
RC {ECO:0000313|EMBL:ABU53200.1}, Rsa42 {ECO:0000313|EMBL:ABU53209.1},
RC Rsa60 {ECO:0000313|EMBL:ABU53210.1}, S578
RC {ECO:0000313|EMBL:ABU53231.1}, S661 {ECO:0000313|EMBL:ABU53229.1},
RC SV16 {ECO:0000313|EMBL:ABU53233.1}, and SV5
RC {ECO:0000313|EMBL:ABU53224.1};
RA Chi F.C., Nolte O.N., Bergmann C.B., Ip M.I., Hakenbeck R.H.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:AAT45179.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2084 {ECO:0000313|EMBL:AAT45179.1}, 2136
RC {ECO:0000313|EMBL:AAT45181.1}, 2146 {ECO:0000313|EMBL:AAT45182.1}, and
RC 2158 {ECO:0000313|EMBL:AAT45183.1};
RX PubMed=19959577; DOI=10.1099/mic.0.035345-0;
RA Leegaard T.M., Bootsma H.J., Caugant D.A., Eleveld M.J., Mannsaker T.,
RA Froholm L.O., Gaustad P., Hoiby E.A., Hermans P.W.;
RT "Phenotypic and genomic characterization of pneumococcus-like streptococci
RT isolated from HIV-seropositive patients.";
RL Microbiology 156:838-848(2010).
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}.
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DR EMBL; AY624698; AAT45179.1; -; Genomic_DNA.
DR EMBL; AY624712; AAT45181.1; -; Genomic_DNA.
DR EMBL; AY624719; AAT45182.1; -; Genomic_DNA.
DR EMBL; AY624726; AAT45183.1; -; Genomic_DNA.
DR EMBL; DQ659957; ABG56207.1; -; Genomic_DNA.
DR EMBL; EU075826; ABU53200.1; -; Genomic_DNA.
DR EMBL; EU075835; ABU53209.1; -; Genomic_DNA.
DR EMBL; EU075836; ABU53210.1; -; Genomic_DNA.
DR EMBL; EU075850; ABU53224.1; -; Genomic_DNA.
DR EMBL; EU075855; ABU53229.1; -; Genomic_DNA.
DR EMBL; EU075857; ABU53231.1; -; Genomic_DNA.
DR EMBL; EU075859; ABU53233.1; -; Genomic_DNA.
DR EMBL; EU075860; ABU53234.1; -; Genomic_DNA.
DR EMBL; AJ617802; CAF02021.1; -; Genomic_DNA.
DR EMBL; AJ617812; CAF02030.1; -; Genomic_DNA.
DR AlphaFoldDB; Q706G3; -.
DR MEROPS; S26.015; -.
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; 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 Hydrolase {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993}.
FT DOMAIN 2..156
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 13
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 51
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAF02030.1"
FT NON_TER 157
FT /evidence="ECO:0000313|EMBL:CAF02030.1"
SQ SEQUENCE 157 AA; 17971 MW; 21269C7F7027D95D CRC64;
IFFWSNVRVE GHSMDPTLAD GEILFVVKHL PIDRFDIVVA HEEDGNKDIV KRVIGMPGDT
IRYENDKLYI NDKETDEPYL ADYIKRFKDD KLQSTYSGKG FEGNKGTFFR SIAEKAQAFT
VDVNYNTNFS FTVPEGEYLL LGDDRLVSSD SRHVGTF
//
