KEGG   PATHWAY: ko03060
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
ko03060

Other DBs
GO: 0043952 0043953
Orthology
K03076  preprotein translocase subunit SecY
K03073  preprotein translocase subunit SecE
K03075  preprotein translocase subunit SecG
K03072  preprotein translocase subunit SecD
K03074  preprotein translocase subunit SecF
K12257  SecD/SecF fusion protein
K03210  preprotein translocase subunit YajC
K03217  YidC/Oxa1 family membrane protein insertase
K03070  preprotein translocase subunit SecA [EC:7.4.2.8]
K03071  preprotein translocase subunit SecB
K13301  secretion monitor
K03106  signal recognition particle subunit SRP54 [EC:3.6.5.4]
K01983  SRP RNA
K03110  fused signal recognition particle receptor
K10956  protein transport protein SEC61 subunit alpha
K09481  protein transport protein SEC61 subunit beta
K07342  protein transport protein SEC61 subunit gamma and related proteins
K12275  translocation protein SEC62
K09540  translocation protein SEC63
K09490  endoplasmic reticulum chaperone BiP [EC:3.6.4.10]
K03109  signal recognition particle subunit SRP9
K03104  signal recognition particle subunit SRP14
K03108  signal recognition particle subunit SRP72
K03107  signal recognition particle subunit SRP68
K03105  signal recognition particle subunit SRP19
K13431  signal recognition particle receptor subunit alpha
K12272  signal recognition particle receptor subunit beta
K03116  sec-independent protein translocase protein TatA
K03117  sec-independent protein translocase protein TatB
K03118  sec-independent protein translocase protein TatC
K03425  sec-independent protein translocase protein TatE
K03100  signal peptidase I [EC:3.4.21.89]
K03101  signal peptidase II [EC:3.4.23.36]
K12946  signal peptidase complex subunit 1 [EC:3.4.-.-]
K12947  signal peptidase complex subunit 2 [EC:3.4.-.-]
K12948  signal peptidase complex subunit 3 [EC:3.4.-.-]
K13280  signal peptidase I [EC:3.4.21.89]
K09647  mitochondrial inner membrane protease subunit 1 [EC:3.4.21.-]
K09648  mitochondrial inner membrane protease subunit 2 [EC:3.4.21.-]
Reference
  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
  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
  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
  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
  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
  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
  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
  Authors
Paetzel M, Karla A, Strynadka NC, Dalbey RE
  Title
Signal peptidases.
  Journal
Chem Rev 102:4549-80 (2002)
DOI:10.1021/cr010166y
Reference
  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
  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
  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
  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
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