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
//