ID G8UQD9_TANFA Unreviewed; 217 AA.
AC G8UQD9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN Name=lepB_5 {ECO:0000313|EMBL:AEW20132.1};
GN OrderedLocusNames=BFO_3099 {ECO:0000313|EMBL:AEW20132.1};
OS Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC
OS 5666 / FDC 338) (Bacteroides forsythus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Tannerella.
OX NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW20132.1, ECO:0000313|Proteomes:UP000005436};
RN [1] {ECO:0000313|Proteomes:UP000005436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43037 / JCM 10827 / CCUG 33226 / KCTC 5666 / FDC 338
RC {ECO:0000313|Proteomes:UP000005436};
RA Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J.,
RA Shetty J., Torralba M., Gill S., Nelson K.;
RT "Complete sequence of Tannerella forsythia ATCC 43037.";
RL Submitted (DEC-2011) 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|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}.
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DR EMBL; CP003191; AEW20132.1; -; Genomic_DNA.
DR RefSeq; WP_014226205.1; NC_016610.1.
DR AlphaFoldDB; G8UQD9; -.
DR STRING; 203275.BFO_3099; -.
DR GeneID; 34759856; -.
DR KEGG; tfo:BFO_3099; -.
DR PATRIC; fig|203275.8.peg.2675; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_1446439_0_0_10; -.
DR Proteomes; UP000005436; Chromosome.
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; 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; 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:AEW20132.1};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000005436}.
FT DOMAIN 8..200
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 33
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 114
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 217 AA; 25299 MW; 5732C480A57CD41F CRC64;
MKQRKGIFFL LLIVSSIFIR IFIGEPTKVS SSSMEPTIKS GDWLWISKVD YGAILPRRWA
DIPILNIVTW IPDFRTKDIR TDWGYCRMRG FNKPDIGDIV VFNSPENIDV LLVKRISQIQ
HANSLIHLDS TNYNNYNDII NQETEAKIKN GVIYINDTIC TYYKLRNNYY YLLGDNSSIS
RDSRFFGYVS EKNLVGKVNR LIFSINKTQI NLLKRVK
//
