ID A0A1L8ZDQ2_BORBI Unreviewed; 326 AA.
AC A0A1L8ZDQ2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=ER70_00275 {ECO:0000313|EMBL:OJH15856.1};
OS Borrelia bissettiae (Borreliella bissettiae).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=64897 {ECO:0000313|EMBL:OJH15856.1, ECO:0000313|Proteomes:UP000183624};
RN [1] {ECO:0000313|EMBL:OJH15856.1, ECO:0000313|Proteomes:UP000183624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO275 {ECO:0000313|EMBL:OJH15856.1,
RC ECO:0000313|Proteomes:UP000183624};
RX PubMed=26419825; DOI=10.1099/mic.0.000192;
RA Leydet B.F.Jr., Liang F.T.;
RT "Similarities in murine infection and immune response to Borrelia bissettii
RT and Borrelia burgdorferi sensu stricto.";
RL Microbiology 161:2352-2360(2015).
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}.
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:OJH15856.1}.
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DR EMBL; JNBW01000018; OJH15856.1; -; Genomic_DNA.
DR RefSeq; WP_071890576.1; NZ_JNBW01000018.1.
DR AlphaFoldDB; A0A1L8ZDQ2; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000183624; 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; cd06530; S26_SPase_I; 2.
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};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 40..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 44..317
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 72
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 159
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 326 AA; 38536 MW; 8F42D2B9CCCDDF57 CRC64;
MYLRRLDKFA SFLVHIVEKY LTYRKRKKYF CKLRAKKRGF LLNFLFDFIA AAIFVLVINQ
YFVQAYKIPS GSMENTLQIG DFLFVDKFSY GPELLPGLFK INGFKVPEES DIIIFENPEY
KSKGVFFDIF QRILYMLTLS FIDLDRDEYG NPNVRFLVKR GVFADGKIVR FNSGKAYIKR
EGEENFILED SYWDLVDKNF KIKKIVANED YGIYGDFAMF IALSQLNINL SSTPDFSFFD
VRMIDRFEFE RLEYKYLSAF MPYVDYYIEK AIIRDYGIYV PYGYVLPIGD NRDNSHDGRF
FGVINKNKVL GRTLIIYLPF SRVGFI
//
