Preprotein translocase subunit SecE - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P0AG96 (SECE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Preprotein translocase subunit SecE

Gene names

Name:	secE
Synonyms:	prlG
Ordered Locus Names:	b3981, JW3944

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	127 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY. Ref.9
Subunit structure	Part of the essential Sec protein translocation complex which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC/OxaA. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. The channel interacts with SecA via subunit SecY. SecE might contact ribosomal protein L23 and/or L29 when the translocation complex is docked with the ribosome. Ref.7 Ref.8
Subcellular location	Cell inner membrane; Multi-pass membrane protein Ref.10.
Post-translational modification	Degraded by FtsH when the SecYEG complex is jammed or upon treatment with antibiotics that block translation elongation such as chloramphenicol.
Disruption phenotype	Essential; deletion experiments lead to loss of the SecYEG tranlocation channel. Leads to loss of translocation of lipoproteins Lpp and BRP. Ref.9
Sequence similarities	Belongs to the SecE/SEC61-gamma family.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular protein transmembrane transport Inferred from mutant phenotype PubMed 3284784. Source: EcoliWiki protein secretion Inferred from electronic annotation. Source: InterPro protein targeting Inferred from electronic annotation. Source: InterPro protein transport by the Sec complex Inferred from mutant phenotype PubMed 3284784. Source: EcoliWiki
Cellular_component	integral to membrane Inferred from direct assay PubMed 9180258. Source: EcoliWiki plasma membrane Inferred from mutant phenotype Ref.1. Source: EcoliWiki
Molecular_function	P-P-bond-hydrolysis-driven protein transmembrane transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 127

127

Preprotein translocase subunit SecE

PRO_0000104163

Regions

Topological domain

1 – 19

Cytoplasmic Probable

Transmembrane

20 – 32

Helical; Probable

Topological domain

33 – 48

Periplasmic Probable

Transmembrane

49 – 60

Helical; Probable

Topological domain

61 – 97

Cytoplasmic Probable

Transmembrane

98 – 115

Helical; Probable

Topological domain

116 – 127

Periplasmic Probable

Experimental info

Mutagenesis

120

S → C: Massive ion flux when cross-linked to SecY C-67 mutation. Ref.12

Sequences

Sequence

Length

Mass (Da)

Tools

P0AG96 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 94D37280522875CE
Show »

FASTA

127

13,643

        10         20         30         40         50         60 
MSANTEAQGS GRGLEAMKWV VVVALLLVAI VGNYLYRDIM LPLRALAVVI LIAAAGGVAL 

        70         80         90        100        110        120 
LTTKGKATVA FAREARTEVR KVIWPTRQET LHTTLIVAAV TAVMSLILWG LDGILVRLVS 


FITGLRF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The secE gene encodes an integral membrane protein required for protein export in Escherichia coli." Schatz P.J., Riggs P.D., Jacq A., Fath M.J., Beckwith J. Genes Dev. 3:1035-1044(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon." Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P. J. Bacteriol. 172:1621-1627(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery." Schatz P.J., Bieker K.L., Ottemann K.M., Silhavy T.J., Beckwith J. EMBO J. 10:1749-1757(1991) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[7]	"Evaluating the oligomeric state of SecYEG in preprotein translocase." Yahr T.L., Wickner W.T. EMBO J. 19:4393-4401(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[8]	"SecYEG assembles into a tetramer to form the active protein translocation channel." Manting E.H., van Der Does C., Remigy H., Engel A., Driessen A.J. EMBO J. 19:852-861(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[9]	"Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway." Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W. J. Biol. Chem. 279:31026-31032(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN LIPOPROTEIN EXPORT, DISRUPTION PHENOTYPE.
[10]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: K12 / MG1655 / ATCC 47076.
[11]	"The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE." Flower A.M., Osborne R.S., Silhavy T.J. EMBO J. 14:884-893(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTANTS.
[12]	"Determining the conductance of the SecY protein translocation channel for small molecules." Saparov S.M., Erlandson K., Cannon K., Schaletzky J., Schulman S., Rapoport T.A., Pohl P. Mol. Cell 26:501-509(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF CHANNEL OPENING, MUTAGENESIS OF SER-120.
[13]	"Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY." van Stelten J., Silva F., Belin D., Silhavy T.J. Science 325:753-756(2009) [PubMed] [Europe PMC] [Abstract] Cited for: COMPLEX DEGRADATION. Strain: K12 / MC4100.
[14]	"Structure of the E. coli protein-conducting channel bound to a translating ribosome." Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J. Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (14.9 ANGSTROMS) OF 17-127 IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN. Strain: MRE-600.
[15]	"Cryo-EM structure of the ribosome-SecYE complex in the membrane environment." Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B., Mielke T., Berninghausen O., Becker T., Schulten K., Beckmann R. Nat. Struct. Mol. Biol. 18:614-621(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN.
[16]	"Protein translocation across the bacterial cytoplasmic membrane." Driessen A.J., Nouwen N. Annu. Rev. Biochem. 77:643-667(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M30610 Genomic DNA. Translation: AAA24621.1.
U00006 Genomic DNA. Translation: AAC43079.1.
U00096 Genomic DNA. Translation: AAC76955.1.
AP009048 Genomic DNA. Translation: BAE77339.1.

PIR

VXECSE. A35139.

RefSeq

NP_418408.1. NC_000913.2.
YP_491480.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AKH	electron microscopy	14.90	C/Z	17-127	[»]
2AKI	electron microscopy	14.90	C/Z	17-127	[»]
3J01	electron microscopy	-	B	12-127	[»]

ProteinModelPortal

P0AG96.

SMR

P0AG96. Positions 12-127.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59303N.

IntAct

P0AG96. 1 interaction.

STRING

511145.b3981.

Protein family/group databases

TCDB

3.A.5.1.1. general secretory pathway (Sec) family.

Proteomic databases

PaxDb

P0AG96.

PRIDE

P0AG96.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76955; AAC76955; b3981.
BAE77339; BAE77339; BAE77339.

GeneID

12930517.
948486.

KEGG

ecj:Y75_p3216.
eco:b3981.

PATRIC

32123483. VBIEscCol129921_4094.

Organism-specific databases

EchoBASE

EB0932.

EcoGene

EG10939. secE.

Phylogenomic databases

eggNOG

COG0690.

HOGENOM

HOG000219148.

K03073.

OMA

WGIDSII.

ProtClustDB

PRK05740.

Enzyme and pathway databases

BioCyc

EcoCyc:SECE.
ECOL316407:JW3944-MONOMER.

Gene expression databases

Genevestigator

P0AG96.

Family and domain databases

InterPro

IPR005807. SecE_bac.
IPR001901. Translocase_SecE/Sec61-g.
[Graphical view]

Pfam

PF00584. SecE. 1 hit.
[Graphical view]

PRINTS

PR01650. SECETRNLCASE.

TIGRFAMs

TIGR00964. secE_bact. 1 hit.

PROSITE

PS01067. SECE_SEC61G. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AG96.

Entry information

Entry name

SECE_ECOLI

Accession

Primary (citable) accession number: P0AG96
Secondary accession number(s): P16920, Q2M8R7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents