ID H6RE92_9BACT Unreviewed; 598 AA.
AC H6RE92;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Signal peptidase I {ECO:0000313|EMBL:CCF99353.1};
DE EC=3.4.21.89 {ECO:0000313|EMBL:CCF99353.1};
GN Name=lepB {ECO:0000313|EMBL:CCF99353.1};
GN ORFNames=VIS_S3BBA60010 {ECO:0000313|EMBL:CCF99353.1};
OS uncultured Cytophagia bacterium.
OC Bacteria; Bacteroidota; Cytophagia; environmental samples.
OX NCBI_TaxID=768505 {ECO:0000313|EMBL:CCF99353.1};
RN [1] {ECO:0000313|EMBL:CCF99353.1}
RP NUCLEOTIDE SEQUENCE.
RA Gomez-Pereira PR, Schuler M, Fuchs BM, Bennke C, Teeling H, Waldmann J,
RA Richter M, Barbe V, Bataille E, Glockner FO, Amann R.;
RT "Genomic content of uncultured Bacteroidetes from contrasting oceanic
RT provinces in the North Atlantic Ocean.";
RL Environ. Microbiol. 14:52-66(2012).
RN [2] {ECO:0000313|EMBL:CCF99353.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370}.
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DR EMBL; FO117577; CCF99353.1; -; Genomic_DNA.
DR AlphaFoldDB; H6RE92; -.
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; 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; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CCF99353.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 163..372
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 512..575
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 192
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 350
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 598 AA; 68403 MW; 767F95A62058CEEB CRC64;
MGVPQILLYL MIVIYFASLW KIFEKAGRQK WEGFVPGYNI WVWLKILNKP WWWIFFFPIP
FVNFVITVAC NVETARMFGK YTPKDTILTV LVPWYMIPAL AYKEENVIVE ATDWTKKGDR
EKRSIHDHLT LFFMAPIIGH ALLVVFRLTG SKDKENKKTM PKEWTDALGF AIVAATIIRV
FFFEAFTIPT GSMEKTMLIG DYLFVNKLKY GAKIPQTPLS VPFVHNRIPG TYTKSYVEWF
KNDYMRLPGY GSIERNDIMV FNWPAGDTVI VHDDAIAHDY YSILRNHAYT MSGQSSYIEF
DKIKDVMMTR AREHIASGGA LYGNPSGGAP ITKTGGVMSH PVDKKENYIK RCVAVGGDTI
EIINGTIHIN GLAEEIPEYA QFNYWFYFKN YEAAIPFSDE YLYENYEIYP SGIQRGEIEV
GDSSTGMKKV NVMIMPCSNR IAAELANLVG VDSASVIWEK KGTDVGYASI FPNDISIDWT
KDNFGPLYIP KEGATIQLNE ENYIAYKRAI TAYEGNTLEK EGDAYLLNGL AATKYTFKQN
YYWLMGDNRH GSADSRYWGY VPEDHVVGTA SFVWFSKTTE KGWFDGGVRW SRIFSFIK
//
