ID A0A142YK82_9PLAN Unreviewed; 590 AA.
AC A0A142YK82;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=signal peptidase I {ECO:0000256|ARBA:ARBA00013208};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208};
GN ORFNames=VT85_19160 {ECO:0000313|EMBL:AMV39564.1};
OS Planctomyces sp. SH-PL62.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctomyces.
OX NCBI_TaxID=1636152 {ECO:0000313|EMBL:AMV39564.1, ECO:0000313|Proteomes:UP000076365};
RN [1] {ECO:0000313|EMBL:AMV39564.1, ECO:0000313|Proteomes:UP000076365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL62 {ECO:0000313|EMBL:AMV39564.1,
RC ECO:0000313|Proteomes:UP000076365};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-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 -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370}.
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; CP011273; AMV39564.1; -; Genomic_DNA.
DR RefSeq; WP_068418847.1; NZ_CP011273.1.
DR AlphaFoldDB; A0A142YK82; -.
DR STRING; 1636152.VT85_19160; -.
DR KEGG; plh:VT85_19160; -.
DR PATRIC; fig|1636152.3.peg.4347; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000076365; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076365};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 149..190
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 65
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 172
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 590 AA; 66319 MW; A4AFC414AE1FF5FC CRC64;
MARSTTATSW RASPSQGPAE GDDEEAARRE TRRNRRESIE SLVVVVVGFL VWSLEAEGFV
IPTGSMAPTL LGRHKEVECP ECGWTYRVNA DCEVEAVGAG GRTGLRVTWG VCENCRFSAR
IDDRPSFAGD RIYTVKSDVA IPLVPGLGRV EPKRWDVTVF KLPEDPTVRY IKRLVGMPGE
VLRIKQGNLW RSDIDDGEAF EILRRPPEES LQVNIPVHDD TYRPRRLASD PRWRRWTSLG
GWEESTPGIY RAASDEGWDE LRYRHVVPSP EQWEALAAGR EPDDPPQPTL ITDFSSFNTD
LAPQNLPQVR FVTRPWFQPH WVGDLALSLR LDVAGPSGRV RIELIEAGVS NRCEIDLATG
EARIFHGDDP LGESRPTAVK ERGSFDLTFA NIDDRLTLWV DGVRPFGDGL AYGSGEGDAY
LTPTVDDLEP ARIAVSGAEV AVGGLVLKRD VYYTQSPGDP DSDDLLDYRG RPPRDLFALL
ADPSRYGGLR WRTPRDYPIE AGRYMMLGDN SSWSRDGRAW TRVDQTTPTA PDRGWDDSGR
ESWEVPRALV IGRAFGVYWA HMRPVWPRFR WGPDLVLPAR PNVEAVRWIY
//
