Protein translocase subunit SecA - Escherichia coli (strain K12)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Protein translocase subunit SecA

Gene names

Name:	secA
Synonyms:	azi, pea, prlD
Ordered Locus Names:	b0098, JW0096

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	901 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. Ref.12
Cofactor	Binds 1 zinc ion per subunit. Zinc is required for binding of the SecB chaperone to the extreme C-terminus of SecA. Ref.7
Subunit structure	Monomer and homodimer; probably dimeric in the cytoplasm. It is not yet clear whether the form that functions in protein insertion is monomeric or dimeric. Part of the essential protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC. Makes direct contact with SecY. Ref.10 Ref.11
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Note: Distribution is 50-50. HAMAP-Rule MF_01382
Induction	Repressed under conditions of excess protein secretion capacity and derepressed when protein secretion becomes limiting. This is regulated by SecM. HAMAP-Rule MF_01382
Disruption phenotype	Essential. Leads to loss of translocation of lipoproteins Lpp and BRP. Ref.12
Sequence similarities	Belongs to the SecA family.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Cell inner membrane Cell membrane Cytoplasm Membrane
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intracellular protein transmembrane transport Inferred from mutant phenotype PubMed 6279567. Source: EcoliWiki protein import Inferred from electronic annotation. Source: InterPro protein targeting Inferred from mutant phenotype PubMed 6279567. Source: EcoliWiki protein transport by the Sec complex Inferred from mutant phenotype PubMed 6279567. Source: EcoliWiki
Cellular_component	cytoplasm Inferred from direct assay PubMed 1837021. Source: EcoliWiki plasma membrane Inferred from direct assay PubMed 1837021. Source: EcoliWiki
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
itself		3	EBI-543213,EBI-543213
lamB	P02943	3	EBI-543213,EBI-371309
secB	P0AG86	4	EBI-543213,EBI-555877
secY	P0AGA2	4	EBI-543213,EBI-761422

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 901

901

Protein translocase subunit SecA HAMAP-Rule MF_01382

PRO_0000109585

Regions

Nucleotide binding

102 – 109

8

ATP Potential

Sites

Metal binding

885

1

Zinc

Metal binding

887

1

Zinc

Metal binding

896

1

Zinc

Metal binding

897

1

Zinc

Experimental info

Sequence conflict

19

1

R → G AA sequence Ref.1

Sequence conflict

737 – 738

2

ER → DG in AAA24619. Ref.1

Sequence conflict

737 – 738

2

ER → DG in CAA38875. Ref.2

Secondary structure

1

.

901

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P10408 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 683D66DD4305DBC2
Show »

FASTA

901

102,023

        10         20         30         40         50         60 
MLIKLLTKVF GSRNDRTLRR MRKVVNIINA MEPEMEKLSD EELKGKTAEF RARLEKGEVL 

        70         80         90        100        110        120 
ENLIPEAFAV VREASKRVFG MRHFDVQLLG GMVLNERCIA EMRTGEGKTL TATLPAYLNA 

       130        140        150        160        170        180 
LTGKGVHVVT VNDYLAQRDA ENNRPLFEFL GLTVGINLPG MPAPAKREAY AADITYGTNN 

       190        200        210        220        230        240 
EYGFDYLRDN MAFSPEERVQ RKLHYALVDE VDSILIDEAR TPLIISGPAE DSSEMYKRVN 

       250        260        270        280        290        300 
KIIPHLIRQE KEDSETFQGE GHFSVDEKSR QVNLTERGLV LIEELLVKEG IMDEGESLYS 

       310        320        330        340        350        360 
PANIMLMHHV TAALRAHALF TRDVDYIVKD GEVIIVDEHT GRTMQGRRWS DGLHQAVEAK 

       370        380        390        400        410        420 
EGVQIQNENQ TLASITFQNY FRLYEKLAGM TGTADTEAFE FSSIYKLDTV VVPTNRPMIR 

       430        440        450        460        470        480 
KDLPDLVYMT EAEKIQAIIE DIKERTAKGQ PVLVGTISIE KSELVSNELT KAGIKHNVLN 

       490        500        510        520        530        540 
AKFHANEAAI VAQAGYPAAV TIATNMAGRG TDIVLGGSWQ AEVAALENPT AEQIEKIKAD 

       550        560        570        580        590        600 
WQVRHDAVLE AGGLHIIGTE RHESRRIDNQ LRGRSGRQGD AGSSRFYLSM EDALMRIFAS 

       610        620        630        640        650        660 
DRVSGMMRKL GMKPGEAIEH PWVTKAIANA QRKVESRNFD IRKQLLEYDD VANDQRRAIY 

       670        680        690        700        710        720 
SQRNELLDVS DVSETINSIR EDVFKATIDA YIPPQSLEEM WDIPGLQERL KNDFDLDLPI 

       730        740        750        760        770        780 
AEWLDKEPEL HEETLRERIL AQSIEVYQRK EEVVGAEMMR HFEKGVMLQT LDSLWKEHLA 

       790        800        810        820        830        840 
AMDYLRQGIH LRGYAQKDPK QEYKRESFSM FAAMLESLKY EVISTLSKVQ VRMPEEVEEL 

       850        860        870        880        890        900 
EQQRRMEAER LAQMQQLSHQ DDDSAAAAAL AAQTGERKVG RNDPCPCGSG KKYKQCHGRL 


Q

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli." Schmidt M., Rollo E., Grodberg J., Oliver D. J. Bacteriol. 170:3404-3414(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[3]	"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.
[4]	"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], SEQUENCE REVISION TO 737-738. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Sequence analysis, transcriptional organization, and insertional mutagenesis of the envA gene of Escherichia coli." Beall B., Lutkenhaus J. J. Bacteriol. 169:5408-5415(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67. Strain: K12.
[6]	"SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli." Lill R., Cunningham K., Brundage L.A., Ito K., Oliver D., Wickner W. EMBO J. 8:961-966(1989) [PubMed] [Europe PMC] [Abstract] Cited for: ATP HYDROLYSIS.
[7]	"Zinc stabilizes the SecB binding site of SecA." Fekkes P., de Wit J.G., Boorsma A., Friesen R.H.E., Driessen A.J.M. Biochemistry 38:5111-5116(1999) [PubMed] [Europe PMC] [Abstract] Cited for: COFACTOR.
[8]	"Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane." Or E., Navon A., Rapoport T. EMBO J. 21:4470-4479(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DIMER DISSOCIATION IN THE PRESENCE OF ACIDIC PHOSPHOLIPIDS, DETERGENTS, SYNTHETIC SIGNAL PEPTIDES.
[9]	"Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase." Duong F. EMBO J. 22:4375-4384(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF MONOMER WITH SECYEG TRANSLOCATION COMPLEX.
[10]	"Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA." Benach J., Chou Y.T., Fak J.J., Itkin A., Nicolae D.D., Smith P.C., Wittrock G., Floyd D.L., Golsaz C.M., Gierasch L.M., Hunt J.F. J. Biol. Chem. 278:3628-3638(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ACIDIC PHOSPHOLIPIDS, SYNTHETIC SIGNAL PEPTIDES, OLIGOMERIZATION STATE OF SECA.
[11]	"Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study." Bu Z., Wang L., Kendall D.A. J. Mol. Biol. 332:23-30(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE TURNOVER, OLIGOMERIZATION STATE OF SECA.
[12]	"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.
[13]	"Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel." Osborne A.R., Rapoport T.A. Cell 129:97-110(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SECY.
[14]	"Preprotein-controlled catalysis in the helicase motor of SecA." Karamanou S., Gouridis G., Papanikou E., Sianidis G., Gelis I., Keramisanou D., Vrontou E., Kalodimos C.G., Economou A. EMBO J. 26:2904-2914(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CONTROL OF ATPASE ACTIVITY.
[15]	"NMR structure of the C-terminal domain of SecA in the free state." Matousek W.M., Alexandrescu A.T. Biochim. Biophys. Acta 1702:163-171(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 880-901.
[16]	"Structure of dimeric SecA, the Escherichia coli preprotein translocase motor." Papanikolau Y., Papadovasilaki M., Ravelli R.B.G., McCarthy A.A., Cusack S., Economou A., Petratos K. J. Mol. Biol. 366:1545-1557(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 9-861 AS A DIMERIC APOPROTEIN, AS A NUCLEOTIDE-BOUND DIMER.
[17]	"Control of SecA and SecM translation by protein secretion." Nakatogawa H., Murakami A., Ito K. Curr. Opin. Microbiol. 7:145-150(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW OF PROTEIN SECRETION CONTROL OF SECA EXPRESSION.
[18]	"Bacterial protein secretion through the translocase nanomachine." Papanikou E., Karamanou S., Economou A. Nat. Rev. Microbiol. 5:839-851(2007) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW OF PROTEIN SECRETION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M20791 Genomic DNA. Translation: AAA24619.1.
M19211 Genomic DNA. Translation: AAA83851.1.
X55034 Genomic DNA. Translation: CAA38875.1.
U00096 Genomic DNA. Translation: AAC73209.1.
AP009048 Genomic DNA. Translation: BAB96666.2.

PIR

BVECCA. B64732.

RefSeq

NP_414640.1. NC_000913.2.
YP_488403.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TM6	NMR	-	A	880-901	[»]
2FSF	X-ray	2.00	A/B	9-861	[»]
2FSG	X-ray	2.20	A/B	9-861	[»]
2FSH	X-ray	2.00	A/B	9-861	[»]
2FSI	X-ray	2.11	A/B	9-861	[»]
2VDA	NMR	-	A	9-836	[»]
3BXZ	X-ray	3.00	A/B	6-609	[»]

ProteinModelPortal

P10408.

SMR

P10408. Positions 9-836.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10840N.

IntAct

P10408. 76 interactions.

MINT

MINT-1224866.

STRING

511145.b0098.

Protein family/group databases

TCDB

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

Proteomic databases

PaxDb

P10408.

PRIDE

P10408.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73209; AAC73209; b0098.
BAB96666; BAB96666; BAB96666.

GeneID

12932123.
944821.

KEGG

ecj:Y75_p0097.
eco:b0098.

PATRIC

32115301. VBIEscCol129921_0102.

Organism-specific databases

EchoBASE

EB0929.

EcoGene

EG10936. secA.

Phylogenomic databases

eggNOG

COG0653.

HOGENOM

HOG000218168.

KO

K03070.

OMA

ERFFILQ.

ProtClustDB

PRK12904.

Enzyme and pathway databases

BioCyc

EcoCyc:SECA.
ECOL316407:JW0096-MONOMER.

Gene expression databases

Genevestigator

P10408.

Family and domain databases

Gene3D

1.10.3060.10. 1 hit.
3.90.1440.10. 1 hit.

HAMAP

MF_01382. SecA.

InterPro

IPR004027. SEC_C_motif.
IPR000185. SecA.
IPR020937. SecA_CS.
IPR011115. SecA_DEAD.
IPR014018. SecA_motor_DEAD.
IPR011130. SecA_preprotein_X-link_dom.
IPR011116. SecA_Wing/Scaffold.
[Graphical view]

Pfam

PF02810. SEC-C. 1 hit.
PF07517. SecA_DEAD. 1 hit.
PF01043. SecA_PP_bind. 1 hit.
PF07516. SecA_SW. 1 hit.
[Graphical view]

PRINTS

PR00906. SECA.

SMART

SM00957. SecA_DEAD. 1 hit.
SM00958. SecA_PP_bind. 1 hit.
[Graphical view]

SUPFAM

SSF81767. SecA_PP_bd. 1 hit.
SSF81886. SecA_SW. 1 hit.

TIGRFAMs

TIGR00963. secA. 1 hit.

PROSITE

PS01312. SECA. 1 hit.
PS51196. SECA_MOTOR_DEAD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P10408.

Entry information

Entry name

SECA_ECOLI

Accession

Primary (citable) accession number: P10408
Secondary accession number(s): P75642

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 136 of the entry and version 2 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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

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