ID G5K2R2_9STRE Unreviewed; 185 AA.
AC G5K2R2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN Name=lepB_2 {ECO:0000313|EMBL:EHI69870.1};
GN ORFNames=STRIC_1079 {ECO:0000313|EMBL:EHI69870.1};
OS Streptococcus ictaluri 707-05.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=764299 {ECO:0000313|EMBL:EHI69870.1, ECO:0000313|Proteomes:UP000003330};
RN [1] {ECO:0000313|EMBL:EHI69870.1, ECO:0000313|Proteomes:UP000003330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=707-05 {ECO:0000313|EMBL:EHI69870.1,
RC ECO:0000313|Proteomes:UP000003330};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
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|RuleBase:RU362042};
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:EHI69870.1}.
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DR EMBL; AEUX02000006; EHI69870.1; -; Genomic_DNA.
DR RefSeq; WP_008089487.1; NZ_AEUX02000006.1.
DR AlphaFoldDB; G5K2R2; -.
DR STRING; 764299.STRIC_1079; -.
DR eggNOG; COG0681; Bacteria.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000003330; 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 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:EHI69870.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000003330};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 8..173
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
SQ SEQUENCE 185 AA; 21253 MW; 590C8A25BC12B982 CRC64;
MVKRDFIRNI LLLLIVIVGA ILLRIFVFST FRVIPETANS YLKSGDLITI KKNIAPKYKD
FVVYKVGKKE YVSRVIALEG DSVTYMDDIF YLNNMVESQS YLEDMKMSFL NKAEPGSLYT
DDFTITTITS GKYESVPKGK YLLLNDNRRN QKDSRQFGLI DASQIKGLVT FRVLPLKEFG
FVEVE
//
