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ENZYME entry: EC 3.4.21.89

Accepted Name
Signal peptidase I.
Alternative Name(s)
Bacterial leader peptidase I.
Phage-procoat-leader peptidase.
SPase I.
Reaction catalysed
Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins
Comment(s)
  • Unaffected by inhibitors of most serine peptidases, but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity.
  • Cleaves a single bond -Ala-|-Ala- in M13 phage procoat protein, producing free signal peptide and coat protein.
  • Eukaryote signal peptidases that may have somewhat different specificity are known from the endoplasmic reticulum membrane and mitochondrial inner membrane.
  • Belongs to peptidase family S26.
  • Formerly EC 3.4.99.36.
Cross-references
PROSITEPDOC00418
BRENDA3.4.21.89
EC2PDB3.4.21.89
ExplorEnz3.4.21.89
PRIAM enzyme-specific profiles3.4.21.89
KEGG Ligand Database for Enzyme Nomenclature3.4.21.89
IUBMB Enzyme Nomenclature3.4.21.89
IntEnz3.4.21.89
MEDLINEFind literature relating to 3.4.21.89
MetaCyc3.4.21.89
UniProtKB/Swiss-Prot
P41026, LEP1_BACAM;  P72660, LEP1_SYNY3;  P41025, LEP2_BACAM;  
P73157, LEP2_SYNY3;  P37943, LEPP_BACNA;  Q57350, LEPQ_BACNA;  
P28628, LEPS_BACSU;  P71013, LEPT_BACSU;  P42959, LEPU_BACSU;  
O07560, LEPV_BACSU;  P54506, LEPW_BACSU;  O67088, LEP_AQUAE;  
P41027, LEP_BACCL;  P42668, LEP_BACLI;  P57347, LEP_BUCAI;  
Q8K9R0, LEP_BUCAP;  Q89AM6, LEP_BUCBP;  P00803, LEP_ECOLI;  
P44454, LEP_HAEIN;  Q9ZLQ5, LEP_HELPJ;  O25300, LEP_HELPY;  
O33021, LEP_MYCLE;  P9WKA0, LEP_MYCTO;  P9WKA1, LEP_MYCTU;  
Q51876, LEP_PHOLA;  Q9I5G7, LEP_PSEAE;  P26844, LEP_PSEFL;  
A8GM78, LEP_RICAH;  A8GYE1, LEP_RICB8;  Q1RHA1, LEP_RICBR;  
A8EXI2, LEP_RICCK;  Q92JB1, LEP_RICCN;  Q4UKA7, LEP_RICFE;  
A8F0M1, LEP_RICM5;  Q9ZE32, LEP_RICPR;  A8GQT7, LEP_RICRS;  
Q8L2J7, LEP_RICTY;  P0A1W3, LEP_SALTI;  P0A1W2, LEP_SALTY;  
Q5HHB9, LEP_STAAC;  P0A067, LEP_STAAM;  P0A068, LEP_STAAN;  
Q6GIC3, LEP_STAAR;  Q6GAW1, LEP_STAAS;  P0A070, LEP_STAAU;  
P0A069, LEP_STAAW;  O07344, LEP_STRPN;  P59662, LEP_STRR6;  
Q8H0W1, PLSP1_ARATH;  P67810, SC11A_BOVIN;  P67811, SC11A_CANLF;  
P67812, SC11A_HUMAN;  Q9R0P6, SC11A_MOUSE;  Q5R9C7, SC11A_PONAB;  
P42667, SC11A_RAT;  P0C7V7, SC11B_HUMAN;  P13679, SC11C_CANLF;  
Q9BY50, SC11C_HUMAN;  Q9D8V7, SC11C_MOUSE;  Q5RC30, SC11C_PONAB;  
Q9WTR7, SC11C_RAT;  F0UDD2, SEC11_AJEC8;  C0NKT8, SEC11_AJECG;  
C6HB29, SEC11_AJECH;  A6QX24, SEC11_AJECN;  C5G8L5, SEC11_AJEDR;  
D4ALL0, SEC11_ARTBC;  E4V4X0, SEC11_ARTGP;  C5FQ45, SEC11_ARTOC;  
Q759W4, SEC11_ASHGO;  A1CL29, SEC11_ASPCL;  B0XWT3, SEC11_ASPFC;  
Q4WYF4, SEC11_ASPFU;  Q2UBW3, SEC11_ASPOR;  Q0CQC5, SEC11_ASPTN;  
C5JJG5, SEC11_BLAGS;  Q5A869, SEC11_CANAL;  C4YNJ0, SEC11_CANAW;  
B9WKT4, SEC11_CANDC;  C5M4J6, SEC11_CANTT;  Q2H1P3, SEC11_CHAGB;  
C4Y3D4, SEC11_CLAL4;  C5PA33, SEC11_COCP7;  E9CXH2, SEC11_COCPS;  
E3QXY4, SEC11_COLGM;  Q6BP15, SEC11_DEBHA;  Q86JD4, SEC11_DICDI;  
Q5B8K4, SEC11_EMENI;  F0XJH4, SEC11_GROCL;  Q6CMR5, SEC11_KLULA;  
C4QXP7, SEC11_KOMPG;  B0D4L0, SEC11_LACBS;  C5DDH1, SEC11_LACTC;  
E5A8D2, SEC11_LEPMJ;  A5DS09, SEC11_LODEL;  A4RGA1, SEC11_MAGO7;  
E9E796, SEC11_METAQ;  E9F8V9, SEC11_METRA;  C7ZHK5, SEC11_NECH7;  
A1D6D8, SEC11_NEOFI;  Q7RY44, SEC11_NEUCR;  E7R7C4, SEC11_OGAPD;  
C1GU90, SEC11_PARBA;  C1FYD2, SEC11_PARBD;  C0S3S0, SEC11_PARBP;  
B6HC89, SEC11_PENRW;  A5DIZ8, SEC11_PICGU;  A3LXS1, SEC11_PICST;  
B2B3T2, SEC11_PODAN;  B2WEL2, SEC11_PYRTR;  E3RR70, SEC11_PYRTT;  
D8Q7Q5, SEC11_SCHCM;  O74323, SEC11_SCHPO;  A7E716, SEC11_SCLS1;  
B6Q5G0, SEC11_TALMQ;  B8M5K5, SEC11_TALSN;  D4D5I1, SEC11_TRIVH;  
D5GNC3, SEC11_TUBMM;  C4JYM4, SEC11_UNCRE;  C9S8G0, SEC11_VERA1;  
Q6CAG9, SEC11_YARLI;  B3LTI7, SEC11_YEAS1;  C7GLT4, SEC11_YEAS2;  
A6ZVU2, SEC11_YEAS7;  C8ZAS4, SEC11_YEAS8;  E7KDY6, SEC11_YEASA;  
E7Q587, SEC11_YEASB;  E7KQ01, SEC11_YEASL;  P15367, SEC11_YEAST;  
E7LVX4, SEC11_YEASV;  E7QG89, SEC11_YEASZ;  C5E3W1, SEC11_ZYGRC;  
O04348, TPP1_ARATH;  Q9M9Z2, TPP2_ARATH;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.21.-
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