GenomeNet

Database: UniProt
Entry: C3K6Y6_PSEFS
LinkDB: C3K6Y6_PSEFS
Original site: C3K6Y6_PSEFS 
ID   C3K6Y6_PSEFS            Unreviewed;       284 AA.
AC   C3K6Y6;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 102.
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};
DE   Flags: Precursor;
GN   Name=lepB {ECO:0000313|EMBL:CAY47323.1};
GN   OrderedLocusNames=PFLU_1059 {ECO:0000313|EMBL:CAY47323.1};
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY47323.1};
RN   [1] {ECO:0000313|EMBL:CAY47323.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAY47323.1};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
RN   [2] {ECO:0000313|EMBL:CAI2795363.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAI2795363.1};
RA   Fortmann-Grote C.;
RL   Submitted (OCT-2023) 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|ARBA:ARBA00000677,
CC         ECO:0000256|RuleBase:RU003993};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU362042}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; OV986001; CAI2795363.1; -; Genomic_DNA.
DR   EMBL; AM181176; CAY47323.1; -; Genomic_DNA.
DR   RefSeq; WP_012722400.1; NC_012660.1.
DR   AlphaFoldDB; C3K6Y6; -.
DR   STRING; 294.SRM1_01038; -.
DR   MEROPS; S26.001; -.
DR   PATRIC; fig|216595.4.peg.1293; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_1_1_6; -.
DR   OrthoDB; 9815782at2; -.
DR   Proteomes; UP001152918; 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; 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, ECO:0000313|EMBL:CAY47323.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993}.
FT   DOMAIN          60..264
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   284 AA;  31859 MW;  5E9336E3505427F1 CRC64;
     MSLNFPLLLV IAVAVCGLLA LLDLVFFAPR RRAAIASYQG SVSQPDGVVI EKLNKEPLLV
     EYGKSFFPVL FIVLVLRSFL VEPFQIPSGS MKPTLDVGDF ILVNKFSYGI RLPVIDKKVI
     EVGDPQRGDV MVFRYPSDPN VNYIKRVVGL PGDVIRYTSD KRLFINGESV AEKLIGSEPN
     SLGSAELYQE KLGAVEHEIR KEMSRYRATP DGEWKVPAGH YFMMGDNRDN SNDSRYWDDP
     NIPKDLLGMV PDQNIVGKAF AVWMSWPEPK LSHLPNFSRV GLIK
//
DBGET integrated database retrieval system