ID A0A127MJH2_9SPHN Unreviewed; 288 AA.
AC A0A127MJH2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AZE99_13240 {ECO:0000313|EMBL:AMO73453.1};
OS Sphingorhabdus sp. M41.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingorhabdus.
OX NCBI_TaxID=1806885 {ECO:0000313|EMBL:AMO73453.1, ECO:0000313|Proteomes:UP000073959};
RN [1] {ECO:0000313|EMBL:AMO73453.1, ECO:0000313|Proteomes:UP000073959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:AMO73453.1,
RC ECO:0000313|Proteomes:UP000073959};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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}; 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; CP014545; AMO73453.1; -; Genomic_DNA.
DR RefSeq; WP_067203689.1; NZ_CP014545.1.
DR AlphaFoldDB; A0A127MJH2; -.
DR STRING; 1806885.AZE99_13240; -.
DR KEGG; sphg:AZE99_13240; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000073959; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042}.
FT DOMAIN 26..251
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 53
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 114
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 288 AA; 30929 MW; 5FF78D24361CBDB1 CRC64;
MALDNIAGSD TAKKPEKEKT DWIGEIKSIA LLLLAVLAFH SLVAKPFYIP SVSMMPGLLV
GDRLIVSKYA YGWSWVSPTF HIVPRVSGRL FGSLPERGDV VILTPREQSS DYIKRVIGLP
GDTIELRGGQ VFLNGIGVRQ DVQPDLQVPI DANSPCGVHE FPGARGVDAD GNPVCNLPIV
RETLPNGVSY DIIDLGPQYT DDVAPVEIPE GQVYLLGDNR DLSADSRVAS PLGLGGPIPW
ENIGGRAEFI TFSLDGTTTL NPLSWWGAFR SGRAGTSLRP AKAVSASK
//
