ID F2L839_BURGS Unreviewed; 297 AA.
AC F2L839;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN OrderedLocusNames=bgla_1g10510 {ECO:0000313|EMBL:AEA59734.1};
OS Burkholderia gladioli (strain BSR3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA59734.1, ECO:0000313|Proteomes:UP000008316};
RN [1] {ECO:0000313|EMBL:AEA59734.1, ECO:0000313|Proteomes:UP000008316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA59734.1,
RC ECO:0000313|Proteomes:UP000008316};
RX PubMed=21478339; DOI=10.1128/JB.00420-11;
RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA Moon J.S., Kim J., Hwang I.;
RT "Complete genome sequence of Burkholderia gladioli BSR3.";
RL J. Bacteriol. 193:3149-3149(2011).
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}.
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DR EMBL; CP002599; AEA59734.1; -; Genomic_DNA.
DR RefSeq; WP_013697085.1; NC_015381.1.
DR AlphaFoldDB; F2L839; -.
DR STRING; 999541.bgla_1g10510; -.
DR MEROPS; S26.001; -.
DR GeneID; 66456942; -.
DR KEGG; bgd:bgla_1g10510; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_1_4; -.
DR Proteomes; UP000008316; Chromosome 1.
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; 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.
DR PROSITE; PS00761; SPASE_I_3; 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 73..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 73..285
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 104
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 159
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 297 AA; 33959 MW; 5B9776ADB3A69E16 CRC64;
MNFALILFVL VVLTGIAWVL DKLVFLPGRR KAADEAAAEF DRQQARVGER FADENAAETR
AKLRDDKLRQ PWWLEYTASF FPVILAVFVV RSFVVEPFKI PSGSMVPTLL VGDFILVNKF
DYGLRLPITN QKITAGRPLA RGDVVVFRYP KDESVDYIKR VIGLPGDTVQ YYDKKLTING
QPVPETPLAD YFDEERMNYA KQYEESIDGR KNAILNNPAV PPFVMGADDF PYKSNCEYNE
HGVTCKVPPG HYFMMGDNRD NSADSRYWGF VPDKDLVGRA FFIWMNFSDL KRIGLFH
//
