ID A0A023Y8S5_9GAMM Unreviewed; 211 AA.
AC A0A023Y8S5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ORFNames=DX03_19185 {ECO:0000313|EMBL:AHY60760.1};
OS Stenotrophomonas rhizophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=216778 {ECO:0000313|EMBL:AHY60760.1, ECO:0000313|Proteomes:UP000025222};
RN [1] {ECO:0000313|EMBL:AHY60760.1, ECO:0000313|Proteomes:UP000025222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14405 {ECO:0000313|Proteomes:UP000025222};
RA Alavi P., Starcher M.R., Thallinger G., Zachow C., Mueller H., Berg G.;
RT "Is there a border between beneficial and pathogenic bacteria?";
RL Submitted (APR-2014) 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:RU362042};
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}.
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DR EMBL; CP007597; AHY60760.1; -; Genomic_DNA.
DR RefSeq; WP_038691186.1; NZ_CP007597.1.
DR AlphaFoldDB; A0A023Y8S5; -.
DR STRING; 216778.DX03_19185; -.
DR GeneID; 61478037; -.
DR HOGENOM; CLU_028723_1_2_6; -.
DR Proteomes; UP000025222; Chromosome.
DR GO; GO:0005886; C:plasma 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};
KW Protease {ECO:0000256|RuleBase:RU362042}.
FT DOMAIN 27..200
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 51
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 211 AA; 22634 MW; E44A6447A3CC22AF CRC64;
MDMPATEPTA APSNRIVHWL KKEALPLAVM LGLLLAARDS LANHYQVPSG SMQHTLMPGD
RVVVDMRAYG LRLPFTSVEL LHTGQPQRGD VAVFDSPVDG IRLIKRIAAV GGDRVELHDG
HLSINGRPLA DASQGEVEDF GQHVAQLDLG QGGGPDITGL TVPDGKVLML GDHRGNSADG
RFFGLVQASA LYGKASHVYY RRGDGLTWQA L
//
