ENTRY ko03060 Pathway NAME Protein export DESCRIPTION The protein export is the active transport of proteins from the cytoplasm to the exterior of the cell, or to the periplasmic compartment in Gram-negative bacteria. The sec dependent pathway is the general protein export system that transports newly synthesized proteins into or across the cell membrane. The translocation channel is formed from a conserved trimeric membrane protein complex, called the Sec61/SecY complex. The twin-arginine translocation (Tat) pathway is another protein transport system that transports folded proteins in bacteria, archaea, and chloroplasts. Many Tat systems comprise three functionally different membrane proteins, TatA, TatB, and TatC, but TatA and TatE seem to have overlapping functions, with TatA having by far the more important role. CLASS Genetic Information Processing; Folding, sorting and degradation PATHWAY_MAP ko03060 Protein export DBLINKS GO: 0043952 0043953 ORTHOLOGY K01551 arsA, ASNA1, GET3; arsenite/tail-anchored protein-transporting ATPase [EC:7.3.2.7 7.3.-.-] K01983 ffs; signal recognition particle 4.5S RNA K03070 secA; preprotein translocase subunit SecA [EC:7.4.2.8] K03071 secB; preprotein translocase subunit SecB K03072 secD; preprotein translocase subunit SecD K03073 secE; preprotein translocase subunit SecE K03074 secF; preprotein translocase subunit SecF K03075 secG; preprotein translocase subunit SecG K03076 secY; preprotein translocase subunit SecY K03100 lepB; signal peptidase I [EC:3.4.21.89] K03101 lspA; signal peptidase II [EC:3.4.23.36] K03104 SRP14; signal recognition particle subunit SRP14 K03105 SRP19; signal recognition particle subunit SRP19 K03106 SRP54, ffh; signal recognition particle subunit SRP54 [EC:3.6.5.4] K03107 SRP68; signal recognition particle subunit SRP68 K03108 SRP72; signal recognition particle subunit SRP72 K03109 SRP9; signal recognition particle subunit SRP9 K03110 ftsY; fused signal recognition particle receptor K03116 tatA; sec-independent protein translocase protein TatA K03117 tatB; sec-independent protein translocase protein TatB K03118 tatC; sec-independent protein translocase protein TatC K03210 yajC; preprotein translocase subunit YajC K03217 yidC, spoIIIJ, OXA1, ccfA; YidC/Oxa1 family membrane protein insertase K03425 tatE; sec-independent protein translocase protein TatE K07342 SEC61G, SSS1, secE; protein transport protein SEC61 subunit gamma and related proteins K09481 SEC61B, SBH2; protein transport protein SEC61 subunit beta K09490 HSPA5, BIP; endoplasmic reticulum chaperone BiP [EC:5.6.1.10] K09540 SEC63, DNAJC23; translocation protein SEC63 K09647 IMP1; mitochondrial inner membrane protease subunit 1 [EC:3.4.21.-] K09648 IMP2; mitochondrial inner membrane protease subunit 2 [EC:3.4.21.-] K10956 SEC61A; protein transport protein SEC61 subunit alpha K12257 secDF; SecD/SecF fusion protein K12272 SRPRB, SRP102; signal recognition particle receptor subunit beta K12275 SEC62; translocation protein SEC62 K12946 SPCS1; signal peptidase complex subunit 1 [EC:3.4.-.-] K12947 SPCS2, SPC2; signal peptidase complex subunit 2 [EC:3.4.-.-] K12948 SPCS3, SPC3; signal peptidase complex subunit 3 [EC:3.4.-.-] K13280 SEC11, sipW; signal peptidase I [EC:3.4.21.89] K13301 secM; secretion monitor K13431 SRPR; signal recognition particle receptor subunit alpha K16365 SGTA; small glutamine-rich tetratricopeptide repeat-containing protein alpha K22384 GET1, WRB; tail-anchored protein insertion receptor K22386 GET2; GET complex subunit GET2 K23387 GET4; golgi to ER traffic protein 4 K23388 UBL4; ubiquitin-like protein 4 K23390 BAG6; large proline-rich protein BAG6 K27163 SND1; SRP-independent targeting protein 1 K27164 SND2, TMEM208; SRP-independent targeting protein 2 K27165 SND3, PHO88; SRP-independent targeting protein 3 REFERENCE PMID:10087917 AUTHORS Dalbey RE, Robinson C. TITLE Protein translocation into and across the bacterial plasma membrane and the plant thylakoid membrane. JOURNAL Trends Biochem Sci 24:17-22 (1999) DOI:10.1016/S0968-0004(98)01333-4 REFERENCE PMID:10652088 AUTHORS Berks BC, Sargent F, Palmer T. TITLE The Tat protein export pathway. JOURNAL Mol Microbiol 35:260-74 (2000) DOI:10.1046/j.1365-2958.2000.01719.x REFERENCE PMID:10747959 AUTHORS Wexler M, Sargent F, Jack RL, Stanley NR, Bogsch EG, Robinson C, Berks BC, Palmer T. TITLE TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export. JOURNAL J Biol Chem 275:16717-22 (2000) DOI:10.1074/jbc.M000800200 REFERENCE PMID:11007775 AUTHORS Jongbloed JD, Martin U, Antelmann H, Hecker M, Tjalsma H, Venema G, Bron S, van Dijl JM, Muller J. TITLE TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway. JOURNAL J Biol Chem 275:41350-7 (2000) DOI:10.1074/jbc.M004887200 REFERENCE PMID:18046402 AUTHORS Rapoport TA TITLE Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. JOURNAL Nature 450:663-9 (2007) DOI:10.1038/nature06384 REFERENCE PMID:17368028 AUTHORS Flower AM TITLE The SecY translocation complex: convergence of genetics and structure. JOURNAL Trends Microbiol 15:203-10 (2007) DOI:10.1016/j.tim.2007.03.001 REFERENCE PMID:16212506 AUTHORS Osborne AR, Rapoport TA, van den Berg B TITLE Protein translocation by the Sec61/SecY channel. JOURNAL Annu Rev Cell Dev Biol 21:529-50 (2005) DOI:10.1146/annurev.cellbio.21.012704.133214 REFERENCE PMID:12475201 AUTHORS Paetzel M, Karla A, Strynadka NC, Dalbey RE TITLE Signal peptidases. JOURNAL Chem Rev 102:4549-80 (2002) DOI:10.1021/cr010166y REFERENCE PMID:10924740 AUTHORS Paetzel M, Dalbey RE, Strynadka NC TITLE The structure and mechanism of bacterial type I signal peptidases. A novel antibiotic target. JOURNAL Pharmacol Ther 87:27-49 (2000) DOI:10.1016/S0163-7258(00)00064-4 REFERENCE PMID:17259602 AUTHORS Ng SY, Chaban B, VanDyke DJ, Jarrell KF TITLE Archaeal signal peptidases. JOURNAL Microbiology 153:305-14 (2007) DOI:10.1099/mic.0.2006/003087-0 REFERENCE PMID:19299134 AUTHORS Desvaux M, Hebraud M, Talon R, Henderson IR TITLE Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. JOURNAL Trends Microbiol 17:139-45 (2009) DOI:10.1016/j.tim.2009.01.004 REFERENCE PMID:15063851 AUTHORS Nakatogawa H, Murakami A, Ito K TITLE Control of SecA and SecM translation by protein secretion. JOURNAL Curr Opin Microbiol 7:145-50 (2004) DOI:10.1016/j.mib.2004.01.001 ///