Preprotein translocase subunit secY - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0AGA2 (SECY_ECOLI)

Last modified December 15, 2009. Version 39. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Preprotein translocase subunit secY

Gene names

Name:	secY
Synonyms:	prlA
Ordered Locus Names:	b3300, JW3262

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Involved in protein export. Interacts with secA and secE to allow the translocation of proteins across the plasma membrane, by forming part of a channel.
Subunit structure	One of seven secretory proteins (secA-F and secY) that comprise the prokaryotic protein translocation apparatus.
Subcellular location	Cell inner membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the secY/SEC61-alpha family.

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Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW transmembrane transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	P-P-bond-hydrolysis-driven protein transmembrane transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
secA	P10408	1	EBI-761422,EBI-543213

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 443

443

Preprotein translocase subunit secY

PRO_0000131721

Regions

Topological domain

1 – 21

Cytoplasmic Probable

Transmembrane

22 – 43

Probable

Topological domain

44 – 77

Periplasmic Probable

Transmembrane

78 – 98

Probable

Topological domain

99 – 121

Cytoplasmic Probable

Transmembrane

122 – 138

Probable

Topological domain

139 – 157

Periplasmic Probable

Transmembrane

158 – 175

Probable

Topological domain

176 – 183

Cytoplasmic Probable

Transmembrane

184 – 205

Probable

Topological domain

206 – 214

Periplasmic Probable

Transmembrane

215 – 238

Probable

Topological domain

239 – 270

Cytoplasmic Probable

Transmembrane

271 – 292

Probable

Topological domain

293 – 313

Periplasmic Probable

Transmembrane

314 – 336

Probable

Topological domain

337 – 371

Cytoplasmic Probable

Transmembrane

372 – 391

Probable

Topological domain

392 – 395

Periplasmic Probable

Transmembrane

396 – 419

Probable

Topological domain

420 – 443

Cytoplasmic Probable

Experimental info

Mutagenesis

P → S in secY100; temperature-sensitive.

Mutagenesis

F → C in prlA3; alterated signal sequence interaction.

Mutagenesis

167

G → E in secY100; temperature-sensitive.

Mutagenesis

240

G → D in secY24; temperature-sensitive.

Mutagenesis

282

S → R in prlA401; alterated signal sequence interaction.

Mutagenesis

286

F → Y in prlA4-1; alterated signal sequence interaction.

Mutagenesis

287

P → L in secY161; alterated signal sequence interaction.

Mutagenesis

290

I → T in secY121; alterated signal sequence interaction.

Mutagenesis

357

R → H in secY39; cold-sensitive.

Mutagenesis

363

A → S in secY40; cold-sensitive.

Mutagenesis

408

I → N in prlA4-2; alterated signal sequence interaction.

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Sequences

Sequence

Length

Mass (Da)

Tools

P0AGA2-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 711CA63CD8809763
Show »

FASTA

443

48,512

        10         20         30         40         50         60 
MAKQPGLDFQ SAKGGLGELK RRLLFVIGAL IVFRIGSFIP IPGIDAAVLA KLLEQQRGTI 

        70         80         90        100        110        120 
IEMFNMFSGG ALSRASIFAL GIMPYISASI IIQLLTVVHP TLAEIKKEGE SGRRKISQYT 

       130        140        150        160        170        180 
RYGTLVLAIF QSIGIATGLP NMPGMQGLVI NPGFAFYFTA VVSLVTGTMF LMWLGEQITE 

       190        200        210        220        230        240 
RGIGNGISII IFAGIVAGLP PAIAHTIEQA RQGDLHFLVL LLVAVLVFAV TFFVVFVERG 

       250        260        270        280        290        300 
QRRIVVNYAK RQQGRRVYAA QSTHLPLKVN MAGVIPAIFA SSIILFPATI ASWFGGGTGW 

       310        320        330        340        350        360 
NWLTTISLYL QPGQPLYVLL YASAIIFFCF FYTALVFNPR ETADNLKKSG AFVPGIRPGE 

       370        380        390        400        410        420 
QTAKYIDKVM TRLTLVGALY ITFICLIPEF MRDAMKVPFY FGGTSLLIVV VVIMDFMAQV 

       430        440 
QTLMMSSQYE SALKKANLKG YGR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene." Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M. Nucleic Acids Res. 11:2599-2616(1983) [PubMed: 6222285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli." Akiyama Y., Ito K. EMBO J. 6:3465-3470(1987) [PubMed: 2828030] [Abstract] Cited for: TOPOLOGY.
[5]	"Biochemical analysis of the biogenesis and function of the Escherichia coli export factor SecY." Swidersky U.E., Rienhoefer-Schweer A., Werner P.K., Ernst F., Benson S.A., Hoffschulte H.K., Mueller M. Eur. J. Biochem. 207:803-811(1992) [PubMed: 1633829] [Abstract] Cited for: CHARACTERIZATION.
[6]	"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: 15919996] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.
[7]	"Structure, function, and biogenesis of SecY, an integral membrane protein involved in protein export." Ito K. J. Bioenerg. Biomembr. 22:353-367(1990) [PubMed: 2202723] [Abstract] Cited for: REVIEW.
[8]	"Temperature-sensitive sec mutants of Escherichia coli: inhibition of protein export at the permissive temperature." Ito K., Hirota Y., Akiyama Y. J. Bacteriol. 171:1742-1743(1989) [PubMed: 2646297] [Abstract] Cited for: MUTANT SECY100.
[9]	"Characterization of cold-sensitive secY mutants of Escherichia coli." Baba T., Jacq A., Brickman E., Beckwith J., Taura T., Ueguchi C., Akiyama Y., Ito K. J. Bacteriol. 172:7005-7010(1990) [PubMed: 2254269] [Abstract] Cited for: MUTANTS SECY39 AND SECY40.
[10]	"Novel prlA alleles defective in supporting staphylokinase processing in Escherichia coli." Sako T. J. Bacteriol. 173:2289-2296(1991) [PubMed: 2007553] [Abstract] Cited for: MUTANTS SECY121 AND SECY161.
[11]	"PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains." Osborne R.S., Silhavy T.J. EMBO J. 12:3391-3398(1993) [PubMed: 8253067] [Abstract] Cited for: MUTANTS.
[12]	"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: 7889938] [Abstract] Cited for: MUTANTS.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X01563 Genomic DNA. Translation: CAA25725.1.
U18997 Genomic DNA. Translation: AAA58097.1.
U00096 Genomic DNA. Translation: AAC76325.1.
AP009048 Genomic DNA. Translation: BAE77991.1.

PIR

QQECSY. A04473.

RefSeq

AP_004490.1.
NP_417759.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AKH	electron microscopy	14.90	B/Y	1-436	[»]
2AKI	electron microscopy	14.90	B/Y	1-436	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AGA2. 1 interaction.

STRING

P0AGA2.

Protein family/group databases

TCDB

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

Genome annotation databases

GeneID

947799.

GenomeReviews

Gene locus JW3262 in contig AP009048_GR.
Gene locus b3300 in contig U00096_GR.

KEGG

ecj:JW3262.
eco:b3300.

Organism-specific databases

EchoBASE

EB0759.

EcoGene

EG10766. secY.

CMR

Search...

Phylogenomic databases

HOGENOM

HBG565931.

OMA

IQTYVIS.

Enzyme and pathway databases

BioCyc

EcoCyc:SECY.
ECOL168927:B3300-MON.

Gene expression databases

Genevestigator

P0AGA2.

Family and domain databases

InterPro

IPR002208. SecY.
[Graphical view]

PANTHER

PTHR10906. SecY. 1 hit.

Pfam

PF00344. SecY. 1 hit.
[Graphical view]

PIRSF

PIRSF004557. SecY. 1 hit.

PRINTS

PR00303. SECYTRNLCASE.

PROSITE

PS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

SECY_ECOLI

Accession

Primary (citable) accession number: P0AGA2
Secondary accession number(s): P03844, Q2M6W5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	December 15, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents