ID L1MJ96_9BACT Unreviewed; 477 AA.
AC L1MJ96;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=signal peptidase I {ECO:0000256|ARBA:ARBA00013208};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208};
GN ORFNames=HMPREF9999_01090 {ECO:0000313|EMBL:EKX91343.1};
OS Alloprevotella sp. oral taxon 473 str. F0040.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=1035197 {ECO:0000313|EMBL:EKX91343.1, ECO:0000313|Proteomes:UP000010460};
RN [1] {ECO:0000313|EMBL:EKX91343.1, ECO:0000313|Proteomes:UP000010460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0040 {ECO:0000313|EMBL:EKX91343.1,
RC ECO:0000313|Proteomes:UP000010460};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKX91343.1}.
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DR EMBL; AMEK01000055; EKX91343.1; -; Genomic_DNA.
DR AlphaFoldDB; L1MJ96; -.
DR STRING; 1035197.HMPREF9999_01090; -.
DR PATRIC; fig|1035197.3.peg.895; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_0_10; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000010460; 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; 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; 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:UP000010460};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..279
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 415..450
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 97
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 248
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 477 AA; 55144 MW; EAE77FE80C0CC055 CRC64;
MLKMPKVTRR QWVLFGVVTA LYLLFLLWVE SWWGLLVVPF IYDLYISRKI NWGWWRTSPD
PIVRTVMSWV DAIVFALVAI YFINQYFFQN FVIPSSSLEK TLLTGDYLLV SKLSYGPRIP
QTPLTMPLTQ HNLPVWLGGG KSYIEWPQWD YRRVKGLGRV QVGDIVVFNY PSGDTVASNF
QNQDYYGLVY STGAQALGIN EPSDSLSPQE QRAAFAKIYG IGQQILKQNA EVGEIISRPV
DRRENYVKRC VAIAGQTLQI KNNDIYVNGK KQARPEHMQL VYNVRFKQAP SVDFLKDNGV
TREDLSRATD GQVISMPLTA QLYNYFKQHP EVATIDGKEP SWNHWLFPLN MAKNWTTSDY
GPVWVPQKGA TIQLTLENLP LYERCIAIYE GNKLQVKDDK IIINDKVANS YTFKMDYYWM
MGDNRDLSAD SRFWGFVPED HIVGKPLMVW LSLDSDYGLF DGKIRWNRTF KWVGDIQ
//
