ID A0A0A2X7R9_THEFI Unreviewed; 268 AA.
AC A0A0A2X7R9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 24-JAN-2024, entry version 40.
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};
GN ORFNames=THFILI_03285 {ECO:0000313|EMBL:KGQ21249.2};
OS Thermus filiformis.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=276 {ECO:0000313|EMBL:KGQ21249.2, ECO:0000313|Proteomes:UP000030364};
RN [1] {ECO:0000313|EMBL:KGQ21249.2, ECO:0000313|Proteomes:UP000030364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43280 {ECO:0000313|EMBL:KGQ21249.2,
RC ECO:0000313|Proteomes:UP000030364};
RA Mandelli F., Ramires B.O., Paixao D.A., Camilo C.M., Polikarpov I.,
RA Couger M.B., Prade R., Riano-Pachon D.M., Squina F.M.;
RT "Draft Genome Sequence of the thermophile Thermus filiformis ATCC43280
RT producer of carotenoid-(di)glucoside-branched fatty acids (di)esters.";
RL Submitted (FEB-2015) 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|ARBA:ARBA00000677,
CC ECO:0000256|RuleBase:RU003993};
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}.
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:KGQ21249.2}.
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DR EMBL; JPSL02000037; KGQ21249.2; -; Genomic_DNA.
DR RefSeq; WP_038066469.1; NZ_JPSL02000037.1.
DR AlphaFoldDB; A0A0A2X7R9; -.
DR STRING; 276.THFILI_03285; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000030364; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 2.
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 Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 9..242
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 40
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 102
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 268 AA; 30640 MW; FEF94B71D19A6EE9 CRC64;
MRAFLEYLWK EWFRQVGEAL LVAFLVTTFV FTTVGVVGQS MFPTLRNGER VLVPKWETWL
VRFGLAEWRR GEIAILKPPE GTPYSVARFP VLGFSFRAFF IKRIVAVPGD EVYVERGVVY
VNGKPLDERH ISDYIQVWPD SFPGACYKDG KLTRVITQQG EFSLALLPPY LKPLVSMLEP
PDEATVERSR LEETCVVGRI RLAKDYYFVM GDNRSLGGSE DSRTFGPVHK SAIAGRASFV
WWPVFVRDEK GIRLNLRSLP VPPAYRLE
//
