ID A1QYI4_BORT9 Unreviewed; 326 AA.
AC A1QYI4;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN OrderedLocusNames=BT0031 {ECO:0000313|EMBL:AAX17376.1};
OS Borrelia turicatae (strain 91E135).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borrelia.
OX NCBI_TaxID=314724 {ECO:0000313|EMBL:AAX17376.1, ECO:0000313|Proteomes:UP000001205};
RN [1] {ECO:0000313|Proteomes:UP000001205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91E135 {ECO:0000313|Proteomes:UP000001205};
RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA Schwan T.G.;
RT "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT comparative analysis of two agents of endemic N. America relapsing fever.";
RL Submitted (DEC-2004) 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|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; CP000049; AAX17376.1; -; Genomic_DNA.
DR RefSeq; WP_011771995.1; NZ_CP073176.1.
DR AlphaFoldDB; A1QYI4; -.
DR KEGG; btu:BT0031; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_847142_0_0_12; -.
DR Proteomes; UP000001205; 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; 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, ECO:0000313|EMBL:AAX17376.1};
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 42..318
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; 38443 MW; 5D6E88C8196B1249 CRC64;
MYLEKLDKFA NFLVKIIEKY LTYRKKRKYF YKLKAKRRGF MLNFLLELLG ASIFVLGINQ
YFLQAYRIPS GSMENTLQIG DLLFVDKFSY GPELLPGVCK INGVKEPNEA EIVIFENVEY
ESKGLFFDIL HRLLYMLSFS FVDLDRDENG NPSVRFLVKR ALFADGKLVR FRNGTVFVRK
EGEESFIEEN SYKASLGYNF GIKKVIEDVD YKVYDNLAMF IALNQLSVDL ENISDFSFFN
VREVDRFEIE RLEYRYLVAF MPYVDYYMEK AIMRDYGIYV PYGYVLPIGD NRDNSYDGRF
FGVINKSKIL GRAFFMYFPF SRIGLI
//
