ID A0A180EP43_9BACT Unreviewed; 536 AA.
AC A0A180EP43;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=signal peptidase I {ECO:0000256|ARBA:ARBA00013208};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208};
GN ORFNames=A3850_011155 {ECO:0000313|EMBL:OAV45010.1};
OS Lewinella sp. 4G2.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC Lewinella.
OX NCBI_TaxID=1803372 {ECO:0000313|EMBL:OAV45010.1, ECO:0000313|Proteomes:UP000076582};
RN [1] {ECO:0000313|EMBL:OAV45010.1, ECO:0000313|Proteomes:UP000076582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G2 {ECO:0000313|EMBL:OAV45010.1,
RC ECO:0000313|Proteomes:UP000076582};
RA Wong S.-K., Yoshizawa S., Ogura Y., Tetsuya H., Nakajima Y., Hamasaki K.;
RT "Lewinella sp. 4G2 Genome sequencing.";
RL Submitted (MAY-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAV45010.1}.
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; LVWJ02000014; OAV45010.1; -; Genomic_DNA.
DR RefSeq; WP_068217187.1; NZ_LVWJ02000014.1.
DR AlphaFoldDB; A0A180EP43; -.
DR STRING; 1803372.A3850_011155; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000076582; Unassembled WGS sequence.
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; 2.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 2.
DR InterPro; IPR043739; DUF5684.
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; IPR019533; Peptidase_S26.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF18936; DUF5684; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 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:UP000076582};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 154..510
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 183
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 305
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 536 AA; 61186 MW; 16525BE2FEBEB4C8 CRC64;
MTWLTLVLLF GYIALSAALY LLFPKAGRDA KLALIPGYNM WIVAEIVGRK GWHSLLLLIP
YFNIFIFAGL MVDLARSFGR YSFGEHVLAV IASWGYFGWV AKQDGPTFVY NGPILEVERQ
YQAELKTATK TGEKREINKV HARYPQFEKP FYQDWAEAAV FAIFAAALIR LLLIESYIIP
TPSMEGNLNV GDFLFVSKVH YGLRLPQTLL MIPLAHNRAP LVGGESYIDG ADLPYRRLPK
IESIDRYDPV VFNVPAGDSV YLIPGRAIYP HDIRHGGNPQ LAQAVESGRL DLITRPVDKR
DHYVKRCVGL PGETLEIRER DVFVNGTKIE DPENVQYSYL VDGVPSTLPE KWRDMKISPD
DFQARGDGRA VMILSNEQKE TLQSQNPGMT FEYTEVPGGV QYYPHDARYW GQQGRDNFGP
VLIPERGMTT KLDEKTYALY WRCIRVYEDN PSFEKRGKKF YLDGQEITEY TFKMDYFWMM
GDNRHNSEDS RVWGFVPEDH ILGKPLFVWF SIKEGSLANG VNWNRIGRSA SKIGGL
//