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Database: UniProt
Entry: A0A3D8LG36_9BACT
LinkDB: A0A3D8LG36_9BACT
Original site: A0A3D8LG36_9BACT 
ID   A0A3D8LG36_9BACT        Unreviewed;       368 AA.
AC   A0A3D8LG36;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN   Name=lepB {ECO:0000313|EMBL:RDV16409.1};
GN   ORFNames=DXT99_04190 {ECO:0000313|EMBL:RDV16409.1};
OS   Pontibacter diazotrophicus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=1400979 {ECO:0000313|EMBL:RDV16409.1, ECO:0000313|Proteomes:UP000256708};
RN   [1] {ECO:0000313|Proteomes:UP000256708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4X {ECO:0000313|Proteomes:UP000256708};
RA   Liu Z.-W., Du Z.-J.;
RL   Submitted (AUG-2018) 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         ECO:0000256|RuleBase:RU362042};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Single-
CC       pass type II membrane protein {ECO:0000256|RuleBase:RU362042}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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:RDV16409.1}.
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DR   EMBL; QRGR01000004; RDV16409.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8LG36; -.
DR   OrthoDB; 9802919at2; -.
DR   Proteomes; UP000256708; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 2.
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; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:RDV16409.1};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256708}.
FT   DOMAIN          23..176
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          303..346
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   368 AA;  42419 MW;  9A4006C9B400E8C5 CRC64;
     MKVKFWEKKP VTKAPKKKKS FAREWGDAII FAVVAASLIR WATFEAYTIP TPSMEKSLLV
     GDFLFVSKLH YGPRTPITPL QVPLTHQTIW GTNIPSYSDA IQLDPHRLPG FSEVQHNDVV
     VFNYPPEEEH PADLRTNYIK RAIGLPGDSL EVRDMQVYIN GNAVNAPEGL QYKYLLVPNT
     QLSEKFFQDR NINLRDVIPY ENGYVVDASP ELAAQMAQLN FITDVILLKD LPGKADPEVF
     PQVPSRYEWN KDNYGPIYIP QEGATVAITP ETLPFYEKII LEYDRNENAE IRDGSLFMNG
     TEVNEYTFKQ NYYFMMGDNR HNSLDSRYWG YVPEDHVVGK AVMIWMSTNP EGTFFDRIRW
     SRLFKTIE
//
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