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Database: UniProt
Entry: W4P9Z9_9BACE
LinkDB: W4P9Z9_9BACE
Original site: W4P9Z9_9BACE 
ID   W4P9Z9_9BACE            Unreviewed;       493 AA.
AC   W4P9Z9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, 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=JCM6292_3034 {ECO:0000313|EMBL:GAE16582.1};
OS   Bacteroides pyogenes JCM 6292.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1235809 {ECO:0000313|EMBL:GAE16582.1, ECO:0000313|Proteomes:UP000018861};
RN   [1] {ECO:0000313|EMBL:GAE16582.1, ECO:0000313|Proteomes:UP000018861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 6292 {ECO:0000313|EMBL:GAE16582.1,
RC   ECO:0000313|Proteomes:UP000018861};
RA   Sakamoto M., Oshima K., Suda W., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Three Strains of Bacteroides pyogenes Isolated
RT   from a Cat and Swine.";
RL   Genome Announc. 2:e01242-13(2014).
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:GAE16582.1}.
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DR   EMBL; BAIQ01000038; GAE16582.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4P9Z9; -.
DR   Proteomes; UP000018861; 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; 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; IPR019533; Peptidase_S26.
DR   PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR   PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR   Pfam; PF10502; Peptidase_S26; 2.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 2.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        63..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..271
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          435..469
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   493 AA;  57495 MW;  BFCA512756D3506C CRC64;
     MIQATRKQWI KFAIVTAIYL AFLIWVRSWW GLIVVPFIFD IYITKKIPWS FWRKSKNAAV
     RTVMSWVDAI VFALVAVYFV NIYIFQNYQI PSSSLEKSLL VGDFLYVSKM SYGPRVPNTP
     LSMPLAQHTL PIVNTKSYIE WPQWKYKRVA GFGRVKLNDI VVFNFPAGDT VALNNQQEDI
     YAIAYQAGRS IYPKEVEMDS LTRNRQRDVY NLYYAAGRKY IDSNPRTFGK VVYRPVDRRE
     NYVKRCVGLP GDTLEIVDGQ VMINGKATVN PENLQFNYFV QTTGPYIPEN MFRDLGISND
     DRILIQNGGW DGELIAMGLD SRDSSGRLNP VYRLPLTKKM YDTLAGNKKL VGKIVKETDS
     YDRKVYPLNL HNRWERNNYG PIWIPSKGAT ITLTDDNLPM YERCITAYEG NKLEVKADGF
     YINGEKTDSY TFRMDYYWMM GDNRDNSLDS RYWGFVPEDH VVGKPIVVWL SLDKDRGWFD
     GRIRWKRLFK WVH
//
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