ID A0A2G2KG98_9PROT Unreviewed; 259 AA.
AC A0A2G2KG98;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN Name=lepB {ECO:0000313|EMBL:PHS09563.1};
GN ORFNames=COA89_01690 {ECO:0000313|EMBL:PHS09563.1};
OS Acidithiobacillus sp.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1872118 {ECO:0000313|EMBL:PHS09563.1, ECO:0000313|Proteomes:UP000221235};
RN [1] {ECO:0000313|Proteomes:UP000221235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) 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:PHS09563.1}.
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DR EMBL; NVVQ01000003; PHS09563.1; -; Genomic_DNA.
DR Proteomes; UP000221235; 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; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
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; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
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};
KW Protease {ECO:0000256|RuleBase:RU362042}.
FT DOMAIN 42..239
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 72
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 259 AA; 29310 MW; 1DC846531190B364 CRC64;
MFSGLVVTGG XVLWDRLQRR TGTDFKDKDT IGAGSRTAGI VIEYARAFFP VILVVFVLRS
FVVEPFRIPS GSMLPSLYIG DFILVSKSSY GIRLPLVNQK IFSIGTPKRG DVMVFRYPHD
EKTNFIKRVV GLPGDIVDYK NKRLRINGNV VDIQKVDRED TEQGXRLSHQ VGEYIESLGK
SSHGILIDAS RRSRDMMRIT VPPDHFFVMG DNRDHSNDSR FWGFVPEENI VGRAFFVWFS
WDSVGGGGVN WPRIGNRID
//
