ID N1W901_9LEPT Unreviewed; 201 AA.
AC N1W901;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN Name=lepB_2 {ECO:0000313|EMBL:EMY71468.1};
GN ORFNames=LEP1GSC199_3598 {ECO:0000313|EMBL:EMY71468.1};
OS Leptospira vanthielii serovar Holland str. Waz Holland = ATCC 700522.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1218591 {ECO:0000313|EMBL:EMY71468.1, ECO:0000313|Proteomes:UP000012227};
RN [1] {ECO:0000313|EMBL:EMY71468.1, ECO:0000313|Proteomes:UP000012227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Waz Holland {ECO:0000313|EMBL:EMY71468.1,
RC ECO:0000313|Proteomes:UP000012227};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Galloway R.L., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (MAR-2013) 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}.
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:EMY71468.1}.
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DR EMBL; AOGY02000014; EMY71468.1; -; Genomic_DNA.
DR AlphaFoldDB; N1W901; -.
DR STRING; 1218591.LEP1GSC199_3598; -.
DR Proteomes; UP000012227; 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; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:EMY71468.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU362042};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 23..200
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 50
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 104
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 201 AA; 23401 MW; 14F4202526448929 CRC64;
MDMETETKVS RWWVKFKRYT RRSLFIFIFL CFLLFVRIFL FQIYSIQGNS MYPTLEHGSV
VFVWKGGFAI SAKFFGTELL YTDPKIDKLD LVLFVSKEEE LVVKRVIGLP GEFYSIEAGR
VLIDSTELLE NYLPKGTYTS EPSTSIFLNR HNSPFLAMDK QGRIPPGYYL LLGDNRQYST
DSRSFGLVPV EKIKGKVIFY F
//