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P0AGD7

- SRP54_ECOLI

UniProt

P0AGD7 - SRP54_ECOLI

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Protein

Signal recognition particle protein

Gene

ffh

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.7 PublicationsUniRule annotation

Enzyme regulationi

Conformation of the Ffh-FtsY complex and regulation of its GTPase activity are modulated by the 4.5S RNA. Formation of the FfH-FtsY complex leads to a mutual stimulation of both GTPases.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 1148GTPUniRule annotation
Nucleotide bindingi190 – 1945GTPUniRule annotation
Nucleotide bindingi248 – 2514GTPUniRule annotation

GO - Molecular functioni

  1. 7S RNA binding Source: InterPro
  2. GTPase activity Source: EcoCyc
  3. GTP binding Source: EcoliWiki

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. protein targeting to membrane Source: EcoliWiki
  3. SRP-dependent cotranslational protein targeting to membrane Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10300-MONOMER.
ECOL316407:JW5414-MONOMER.

Protein family/group databases

TCDBi3.A.5.1.1. the general secretory pathway (sec) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle proteinUniRule annotation
Alternative name(s):
Fifty-four homologUniRule annotation
Short name:
Ffh
p48
Gene namesi
Name:ffhUniRule annotation
Ordered Locus Names:b2610, JW5414
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10300. ffh.

Subcellular locationi

Cytoplasm
Note: The SRP-RNC complex is targeted to the cytoplasmic membrane.

GO - Cellular componenti

  1. ribonucleoprotein complex Source: EcoliWiki
  2. signal recognition particle Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Signal recognition particle

Pathology & Biotechi

Disruption phenotypei

Essential; deletion experiments lead to loss of inner membrane protein targeting. Also leads to reduced targeting of lipoproteins Lpp and BRP.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Signal recognition particle proteinPRO_0000101153Add
BLAST

Proteomic databases

PaxDbiP0AGD7.
PRIDEiP0AGD7.

Expressioni

Gene expression databases

GenevestigatoriP0AGD7.

Interactioni

Subunit structurei

Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY. SRP is a ribonucleoprotein composed of Ffh and a 4.5S RNA molecule. Metal ions are essential for the formation and stability of the SRP complex. Interacts with the ribosomes, via ribosomal protein L23. Interacts with FtsY.7 PublicationsUniRule annotation

Protein-protein interaction databases

DIPiDIP-31865N.
IntActiP0AGD7. 19 interactions.
MINTiMINT-1218614.
STRINGi511145.b2610.

Structurei

Secondary structure

1
453
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1511Combined sources
Helixi24 – 4017Combined sources
Helixi45 – 6016Combined sources
Helixi70 – 8617Combined sources
Beta strandi96 – 10611Combined sources
Helixi113 – 12614Combined sources
Beta strandi132 – 1365Combined sources
Helixi144 – 15512Combined sources
Beta strandi158 – 1603Combined sources
Helixi168 – 18114Combined sources
Beta strandi185 – 1906Combined sources
Helixi199 – 21214Combined sources
Beta strandi215 – 2228Combined sources
Helixi229 – 23911Combined sources
Beta strandi244 – 2485Combined sources
Helixi258 – 2669Combined sources
Beta strandi270 – 2745Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi282 – 2843Combined sources
Helixi287 – 2959Combined sources
Helixi331 – 3388Combined sources
Helixi373 – 3819Combined sources
Helixi385 – 3895Combined sources
Helixi391 – 3933Combined sources
Helixi396 – 40510Combined sources
Helixi410 – 43021Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DULX-ray1.80A329-430[»]
1HQ1X-ray1.52A328-432[»]
2J28electron microscopy8.0092-431[»]
2PXBX-ray2.00A329-430[»]
2PXDX-ray2.00A329-430[»]
2PXEX-ray2.00A329-430[»]
2PXFX-ray2.00A329-430[»]
2PXKX-ray2.00A329-430[»]
2PXLX-ray2.50A329-430[»]
2PXPX-ray2.50A329-430[»]
2PXQX-ray2.50A329-430[»]
2PXTX-ray2.50A329-430[»]
2PXUX-ray2.50A329-430[»]
2PXVX-ray2.00A329-430[»]
2XKVelectron microscopy13.50C329-430[»]
2XXAX-ray3.94A/C1-433[»]
3LQXX-ray1.93A329-428[»]
4C7OX-ray2.60A/C1-298[»]
ProteinModelPortaliP0AGD7.
SMRiP0AGD7. Positions 2-431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AGD7.

Family & Domainsi

Domaini

Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.2 PublicationsUniRule annotation

Sequence similaritiesi

Belongs to the GTP-binding SRP family. SRP54 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0541.
HOGENOMiHOG000036164.
InParanoidiP0AGD7.
KOiK03106.
OMAiMLPGMGQ.
OrthoDBiEOG62K1ZH.
PhylomeDBiP0AGD7.

Family and domain databases

Gene3Di1.10.260.30. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00306. SRP54.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004125. Signal_recog_particle_SRP54_M.
IPR022941. SRP54.
IPR000897. SRP54_GTPase_dom.
IPR004780. SRP_Ffh.
[Graphical view]
PANTHERiPTHR11564:SF7. PTHR11564:SF7. 1 hit.
PfamiPF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
PF02978. SRP_SPB. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMiSSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00959. ffh. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AGD7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFDNLTDRLS RTLRNISGRG RLTEDNVKDT LREVRMALLE ADVALPVVRE 
        60         70         80         90        100
FINRVKEKAV GHEVNKSLTP GQEFVKIVRN ELVAAMGEEN QTLNLAAQPP 
       110        120        130        140        150
AVVLMAGLQG AGKTTSVGKL GKFLREKHKK KVLVVSADVY RPAAIKQLET 
       160        170        180        190        200
LAEQVGVDFF PSDVGQKPVD IVNAALKEAK LKFYDVLLVD TAGRLHVDEA 
       210        220        230        240        250
MMDEIKQVHA SINPVETLFV VDAMTGQDAA NTAKAFNEAL PLTGVVLTKV 
       260        270        280        290        300
DGDARGGAAL SIRHITGKPI KFLGVGEKTE ALEPFHPDRI ASRILGMGDV 
       310        320        330        340        350
LSLIEDIESK VDRAQAEKLA SKLKKGDGFD LNDFLEQLRQ MKNMGGMASL 
       360        370        380        390        400
MGKLPGMGQI PDNVKSQMDD KVLVRMEAII NSMTMKERAK PEIIKGSRKR 
       410        420        430        440        450
RIAAGCGMQV QDVNRLLKQF DDMQRMMKKM KKGGMAKMMR SMKGMMPPGF 

PGR
Length:453
Mass (Da):49,787
Last modified:December 20, 2005 - v1
Checksum:iE9C7A7101CC04D66
GO

Sequence cautioni

The sequence CAA25957.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01818 Genomic DNA. Translation: CAA25957.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75659.1.
AP009048 Genomic DNA. Translation: BAA16495.2.
PIRiE65039.
RefSeqiNP_417101.1. NC_000913.3.
YP_490833.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75659; AAC75659; b2610.
BAA16495; BAA16495; BAA16495.
GeneIDi12933092.
947102.
KEGGiecj:Y75_p2558.
eco:b2610.
PATRICi32120619. VBIEscCol129921_2708.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 X01818 Genomic DNA. Translation: CAA25957.1 . Different initiation.
U00096 Genomic DNA. Translation: AAC75659.1 .
AP009048 Genomic DNA. Translation: BAA16495.2 .
PIRi E65039.
RefSeqi NP_417101.1. NC_000913.3.
YP_490833.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DUL X-ray 1.80 A 329-430 [» ]
1HQ1 X-ray 1.52 A 328-432 [» ]
2J28 electron microscopy 8.00 9 2-431 [» ]
2PXB X-ray 2.00 A 329-430 [» ]
2PXD X-ray 2.00 A 329-430 [» ]
2PXE X-ray 2.00 A 329-430 [» ]
2PXF X-ray 2.00 A 329-430 [» ]
2PXK X-ray 2.00 A 329-430 [» ]
2PXL X-ray 2.50 A 329-430 [» ]
2PXP X-ray 2.50 A 329-430 [» ]
2PXQ X-ray 2.50 A 329-430 [» ]
2PXT X-ray 2.50 A 329-430 [» ]
2PXU X-ray 2.50 A 329-430 [» ]
2PXV X-ray 2.00 A 329-430 [» ]
2XKV electron microscopy 13.50 C 329-430 [» ]
2XXA X-ray 3.94 A/C 1-433 [» ]
3LQX X-ray 1.93 A 329-428 [» ]
4C7O X-ray 2.60 A/C 1-298 [» ]
ProteinModelPortali P0AGD7.
SMRi P0AGD7. Positions 2-431.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31865N.
IntActi P0AGD7. 19 interactions.
MINTi MINT-1218614.
STRINGi 511145.b2610.

Protein family/group databases

TCDBi 3.A.5.1.1. the general secretory pathway (sec) family.

Proteomic databases

PaxDbi P0AGD7.
PRIDEi P0AGD7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75659 ; AAC75659 ; b2610 .
BAA16495 ; BAA16495 ; BAA16495 .
GeneIDi 12933092.
947102.
KEGGi ecj:Y75_p2558.
eco:b2610.
PATRICi 32120619. VBIEscCol129921_2708.

Organism-specific databases

EchoBASEi EB0296.
EcoGenei EG10300. ffh.

Phylogenomic databases

eggNOGi COG0541.
HOGENOMi HOG000036164.
InParanoidi P0AGD7.
KOi K03106.
OMAi MLPGMGQ.
OrthoDBi EOG62K1ZH.
PhylomeDBi P0AGD7.

Enzyme and pathway databases

BioCyci EcoCyc:EG10300-MONOMER.
ECOL316407:JW5414-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AGD7.
PROi P0AGD7.

Gene expression databases

Genevestigatori P0AGD7.

Family and domain databases

Gene3Di 1.10.260.30. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_00306. SRP54.
InterProi IPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004125. Signal_recog_particle_SRP54_M.
IPR022941. SRP54.
IPR000897. SRP54_GTPase_dom.
IPR004780. SRP_Ffh.
[Graphical view ]
PANTHERi PTHR11564:SF7. PTHR11564:SF7. 1 hit.
Pfami PF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
PF02978. SRP_SPB. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00959. ffh. 1 hit.
PROSITEi PS00300. SRP54. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide."
    Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.
    EMBO J. 2:899-905(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle."
    Ribes V., Roemisch K., Giner A., Dobberstein B., Tollervey D.
    Cell 63:591-600(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex."
    Luirink J., High S., Wood H., Giner A., Tollervey D., Dobberstein B.
    Nature 359:741-743(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  7. "The E. coli ffh gene is necessary for viability and efficient protein export."
    Phillips G.J., Silhavy T.J.
    Nature 359:744-746(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  8. "Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor."
    Powers T., Walter P.
    EMBO J. 16:4880-4886(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  9. "Role of SRP RNA in the GTPase cycles of Ffh and FtsY."
    Peluso P., Shan S.O., Nock S., Herschlag D., Walter P.
    Biochemistry 40:15224-15233(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GTPASE ACTIVITY, ENZYME REGULATION.
  10. "Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway."
    Tian H., Beckwith J.
    J. Bacteriol. 184:111-118(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: K12.
  11. "Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome."
    Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J.
    J. Cell Biol. 161:679-684(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIBOSOMAL PROTEIN L23 AND NASCENT PROTEIN CHAINS.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  12. "The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome."
    Gu S.-Q., Peske F., Wieden H.-J., Rodnina M.V., Wintermeyer W.
    RNA 9:566-573(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIBOSOMAL PROTEIN L23, DOMAIN.
    Strain: MRE-600.
  13. "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.
  14. "Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor."
    Buskiewicz I., Deuerling E., Gu S.-Q., Joeckel J., Rodnina M.V., Bukau B., Wintermeyer W.
    Proc. Natl. Acad. Sci. U.S.A. 101:7902-7906(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMULTANEOUS BINDING OF TRIGGER FACTOR AND SRP TO THE RIBOSOME.
    Strain: MRE-600.
  15. "Early targeting events during membrane protein biogenesis in Escherichia coli."
    Bibi E.
    Biochim. Biophys. Acta 1808:841-850(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. "Structure of a methionine-rich segment of Escherichia coli Ffh protein."
    Oh D.-B., Yi G.-S., Chi S.-W., Kim H.
    FEBS Lett. 395:160-164(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 410-434.
  17. "Crystal structure of the ribonucleoprotein core of the signal recognition particle."
    Batey R.T., Rambo R.P., Lucast L., Rha B., Doudna J.A.
    Science 287:1232-1239(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 371-430 IN COMPLEX WITH 4.5S RNA, DOMAIN.
  18. "Structural and energetic analysis of metal ions essential to SRP signal recognition domain assembly."
    Batey R.T., Doudna J.A.
    Biochemistry 41:11703-11710(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 328-432, SUBUNIT.
  19. "Following the signal sequence from ribosomal tunnel exit to signal recognition particle."
    Halic M., Blau M., Becker T., Mielke T., Pool M.R., Wild K., Sinning I., Beckmann R.
    Nature 444:507-511(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (8.00 ANGSTROMS) OF 2-431.
  20. "A general strategy to solve the phase problem in RNA crystallography."
    Keel A.Y., Rambo R.P., Batey R.T., Kieft J.S.
    Structure 15:761-772(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 329-430.
  21. "Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor."
    Estrozi L.F., Boehringer D., Shan S.O., Ban N., Schaffitzel C.
    Nat. Struct. Mol. Biol. 18:88-90(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (13.50 ANGSTROMS) OF 371-430.
  22. "The crystal structure of the signal recognition particle in complex with its receptor."
    Ataide S.F., Schmitz N., Shen K., Ke A., Shan S.O., Doudna J.A., Ban N.
    Science 331:881-886(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.94 ANGSTROMS) OF 1-433.
+Additional computationally mapped references.

Entry informationi

Entry nameiSRP54_ECOLI
AccessioniPrimary (citable) accession number: P0AGD7
Secondary accession number(s): P07019, P77007, P77008
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 20, 2005
Last modified: January 7, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
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