ID E6YYC4_BARSR Unreviewed; 261 AA.
AC E6YYC4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 13-SEP-2023, entry version 45.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN Name=lepB {ECO:0000313|EMBL:CBI81935.1};
GN ORFNames=B11C_20212 {ECO:0000313|EMBL:CBI81935.1};
OS Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=687861 {ECO:0000313|EMBL:CBI81935.1};
RN [1] {ECO:0000313|EMBL:CBI81935.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R1 {ECO:0000313|EMBL:CBI81935.1};
RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT "Parallel evolution of a type IV secretion system in radiating lineages of
RT the host-restricted bacterial pathogen Bartonella.";
RL PLoS Genet. 7:E1001296-E1001296(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: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; FN645507; CBI81935.1; -; Genomic_DNA.
DR AlphaFoldDB; E6YYC4; -.
DR MEROPS; S26.001; -.
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, ECO:0000313|EMBL:CBI81935.1};
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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 19..223
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 48
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 109
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 261 AA; 29830 MW; 06459FAD21221A00 CRC64;
MMSQKEKVQK KKEKGGVFEL ISVLIQALFL AVLIRTLFFQ PFTIPSGSMR PTLLVGDYLF
VSKYAYGYSR FSLPFSPPIF SGRIWASQPK RGDVVVFRLP SNPSVDYIKR VVGLPGDYVQ
VRQGVLYIND KAVSRQLMGQ IDDADVTELN RPVDVYRETL SNGVSYNTLD LGFFPQVDNT
KVFEVPPGHY FMMGDNRHNS DDSRLGVGYV PEENLVGRAN LIFFSISNGS SAWQIWRWPF
DVRWARLFSF VNTIHYFPLT K
//
