ID Q67PD6_SYMTH Unreviewed; 189 AA.
AC Q67PD6;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 112.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN OrderedLocusNames=STH1472 {ECO:0000313|EMBL:BAD40457.1};
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD40457.1, ECO:0000313|Proteomes:UP000000417};
RN [1] {ECO:0000313|EMBL:BAD40457.1, ECO:0000313|Proteomes:UP000000417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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: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|RuleBase:RU362042}; Single-pass type II membrane
CC protein {ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP006840; BAD40457.1; -; Genomic_DNA.
DR RefSeq; WP_011195602.1; NC_006177.1.
DR AlphaFoldDB; Q67PD6; -.
DR STRING; 292459.STH1472; -.
DR KEGG; sth:STH1472; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_5_1_9; -.
DR OMA; RAEFIFW; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000000417; 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; IPR019758; Pept_S26A_signal_pept_1_CS.
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; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000000417};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 18..172
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 48
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 92
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 189 AA; 20883 MW; 9AE83D4D52534269 CRC64;
MADVPDERPA VRRKSPLREV LETLVLALLF ALIIRTFVVE VYQVSGSSMT NTLYDQERVL
VNKFIYKLVR DPRPGDIIVF KYPRQPERDF IKRVVAVAGD TVEMRGGVVY VNGEPFNEAP
TVRLSAGDFG PVVVPPDSVF VLGDNRSNSE DSRYFGEVPL SHIRGLAVAR IWPLTEISAL
ALPAAEGGG
//