ID I0I7R2_CALAS Unreviewed; 193 AA.
AC I0I7R2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=CLDAP_32600 {ECO:0000313|EMBL:BAM01300.1};
OS Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS STL-6-O1).
OC Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC Caldilinea.
OX NCBI_TaxID=926550 {ECO:0000313|EMBL:BAM01300.1, ECO:0000313|Proteomes:UP000007880};
RN [1] {ECO:0000313|EMBL:BAM01300.1, ECO:0000313|Proteomes:UP000007880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC {ECO:0000313|Proteomes:UP000007880};
RA Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Hanada S., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT 102666).";
RL Submitted (FEB-2012) 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: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; AP012337; BAM01300.1; -; Genomic_DNA.
DR AlphaFoldDB; I0I7R2; -.
DR STRING; 926550.CLDAP_32600; -.
DR KEGG; cap:CLDAP_32600; -.
DR PATRIC; fig|926550.5.peg.3525; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_5_1_0; -.
DR Proteomes; UP000007880; Chromosome.
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; 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; IPR019757; Pept_S26A_signal_pept_1_Lys-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; PS00760; SPASE_I_2; 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:UP000007880};
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 19..172
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 47
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 90
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 193 AA; 22142 MW; E5E5DD566AFAF0FE CRC64;
MDAEATRNEP AYGWMMVREI VETVVLSLII FLLIRQVVQN YRIENHSMEP SFYEGQFVLV
NKVAYWFSEP KRGDVIVFHN PRNTREDYIK RVIGIPGDTV EVRDQKVFVN GMPLPEEYPH
RPIPPGEYAG PFVVGENQLF VMGDNRPNSS DSRVFGPIDR SLVVGQAWLR IWPLNVFGIV
QHADLAPEGY LPD
//
