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Database: UniProt
Entry: A0A180EP43_9BACT
LinkDB: A0A180EP43_9BACT
Original site: A0A180EP43_9BACT 
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}.
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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
//
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