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UniProtKB - P0AGD7 (SRP54_ECOLI)

Entry version 131 (08 May 2019)
Sequence version 1 (20 Dec 2005)
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Protein

Signal recognition particle protein

Gene

ffh

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.UniRule annotation7 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi107 – 114GTPUniRule annotation8
Nucleotide bindingi190 – 194GTPUniRule annotation5
Nucleotide bindingi248 – 251GTPUniRule annotation4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • 7S RNA binding Source: InterPro
  • GTPase activity Source: EcoCyc
  • GTP binding Source: EcoliWiki
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRibonucleoprotein, RNA-binding
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

Protein family/group databases

Transport Classification Database

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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Signal recognition particle proteinUniRule annotation
Alternative name(s):
Fifty-four homologUniRule annotation
Short name:
Ffh
p48
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ffhUniRule annotation
Ordered Locus Names:b2610, JW5414
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10300 ffh

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cytoplasm, Signal recognition particle

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001011531 – 453Signal recognition particle proteinAdd BLAST453

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0AGD7

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0AGD7

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P0AGD7

PRoteomics IDEntifications database

More...PRIDEi		P0AGD7

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.UniRule annotation7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4262086, 316 interactors

Database of interacting proteins

More...DIPi		DIP-31865N

Protein interaction database and analysis system

More...IntActi		P0AGD7, 22 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2610

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DULX-ray1.80A371-430[»]
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 microscopy13.50C371-430[»]
2XXAX-ray3.94A/C1-433[»]
3LQXX-ray1.93A329-428[»]
4C7OX-ray2.60A/C1-298[»]
5AKAelectron microscopy5.705328-436[»]
5GADelectron microscopy3.70i4-434[»]
5GAFelectron microscopy4.30i1-434[»]
5GAGelectron microscopy3.80i4-434[»]
5GAHelectron microscopy3.80i1-434[»]
5NCOelectron microscopy4.80i4-434[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P0AGD7

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0AGD7

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.UniRule annotation2 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105CB9 Bacteria
COG0541 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000036164

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0AGD7

KEGG Orthology (KO)

More...KOi		K03106

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0AGD7

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.260.30, 1 hit
1.20.120.140, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00306 SRP54, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003593 AAA+_ATPase
IPR027417 P-loop_NTPase
IPR036891 Signal_recog_part_SRP54_M_sf
IPR013822 Signal_recog_particl_SRP54_hlx
IPR004125 Signal_recog_particle_SRP54_M
IPR004780 SRP
IPR022941 SRP54
IPR000897 SRP54_GTPase_dom
IPR042101 SRP54_N_sf

The PANTHER Classification System

More...PANTHERi		PTHR11564 PTHR11564, 1 hit
PTHR11564:SF7 PTHR11564:SF7, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00448 SRP54, 1 hit
PF02881 SRP54_N, 1 hit
PF02978 SRP_SPB, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00382 AAA, 1 hit
SM00962 SRP54, 1 hit
SM00963 SRP54_N, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47446 SSF47446, 1 hit
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00959 ffh, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00300 SRP54, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE9C7A7101CC04D66
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X01818 Genomic DNA Translation: CAA25957.1 Different initiation.
U00096 Genomic DNA Translation: AAC75659.1
AP009048 Genomic DNA Translation: BAA16495.2

Protein sequence database of the Protein Information Resource

More...PIRi		E65039

NCBI Reference Sequences

More...RefSeqi		NP_417101.1, NC_000913.3
WP_000460035.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75659; AAC75659; b2610
BAA16495; BAA16495; BAA16495

Database of genes from NCBI RefSeq genomes

More...GeneIDi		947102

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW5414
eco:b2610

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.4129

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PIRiE65039
RefSeqiNP_417101.1, NC_000913.3
WP_000460035.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DULX-ray1.80A371-430[»]
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 microscopy13.50C371-430[»]
2XXAX-ray3.94A/C1-433[»]
3LQXX-ray1.93A329-428[»]
4C7OX-ray2.60A/C1-298[»]
5AKAelectron microscopy5.705328-436[»]
5GADelectron microscopy3.70i4-434[»]
5GAFelectron microscopy4.30i1-434[»]
5GAGelectron microscopy3.80i4-434[»]
5GAHelectron microscopy3.80i1-434[»]
5NCOelectron microscopy4.80i4-434[»]
SMRiP0AGD7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262086, 316 interactors
DIPiDIP-31865N
IntActiP0AGD7, 22 interactors
STRINGi511145.b2610

Protein family/group databases

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

Proteomic databases

EPDiP0AGD7
jPOSTiP0AGD7
PaxDbiP0AGD7
PRIDEiP0AGD7

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75659; AAC75659; b2610
BAA16495; BAA16495; BAA16495
GeneIDi947102
KEGGiecj:JW5414
eco:b2610
PATRICifig|1411691.4.peg.4129

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0296
EcoGeneiEG10300 ffh

Phylogenomic databases

eggNOGiENOG4105CB9 Bacteria
COG0541 LUCA
HOGENOMiHOG000036164
InParanoidiP0AGD7
KOiK03106
PhylomeDBiP0AGD7

Enzyme and pathway databases

BioCyciEcoCyc:EG10300-MONOMER
ECOL316407:JW5414-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AGD7

Protein Ontology

More...PROi		PR:P0AGD7

Family and domain databases

Gene3Di1.10.260.30, 1 hit
1.20.120.140, 1 hit
HAMAPiMF_00306 SRP54, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR027417 P-loop_NTPase
IPR036891 Signal_recog_part_SRP54_M_sf
IPR013822 Signal_recog_particl_SRP54_hlx
IPR004125 Signal_recog_particle_SRP54_M
IPR004780 SRP
IPR022941 SRP54
IPR000897 SRP54_GTPase_dom
IPR042101 SRP54_N_sf
PANTHERiPTHR11564 PTHR11564, 1 hit
PTHR11564:SF7 PTHR11564:SF7, 1 hit
PfamiView protein in Pfam
PF00448 SRP54, 1 hit
PF02881 SRP54_N, 1 hit
PF02978 SRP_SPB, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SM00962 SRP54, 1 hit
SM00963 SRP54_N, 1 hit
SUPFAMiSSF47446 SSF47446, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00959 ffh, 1 hit
PROSITEiView protein in PROSITE
PS00300 SRP54, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSRP54_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0AGD7
Secondary accession number(s): P07019, P77007, P77008
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 20, 2005
Last modified: May 8, 2019
This is version 131 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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