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UniProtKB - P06971 (FHUA_ECOLI)

Protein

Ferrichrome outer membrane transporter/phage receptor

Gene

fhuA

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 the uptake of iron in complex with ferrichrome, an hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane (PubMed:1089064, PubMed:2066336). In addition to its role in ferrichrome-iron transport, transports the antibiotic albomycin, which is a structural analog of ferrichrome, and acts as a receptor for colicin M, microcin J25 and bacteriophages T1, T5, phi80 and UC-1 (PubMed:1089064, PubMed:353030, PubMed:2066336, PubMed:8617231). The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system (PubMed:353030, PubMed:9353297, PubMed:12427941).6 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

Binding of ferrichrome or colicin M enhances the interaction between FhuA and TonB (PubMed:9353297). TonB activates FhuA through interaction with the beta-barrel (PubMed:12427941).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei114Ferrichrome3 Publications1
Binding sitei133Ferrichrome3 Publications1
Binding sitei424Ferrichrome1 Publication1
Binding sitei735Ferrichrome1 Publication1

<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

  • cofactor binding Source: EcoliWiki
  • iron ion binding Source: EcoliWiki
  • protein domain specific binding Source: CAFA
  • siderophore uptake transmembrane transporter activity Source: GO_Central
  • signaling receptor activity Source: InterPro
  • toxic substance binding Source: EcoliWiki
  • virion 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 functionReceptor
Biological processIon transport, Iron transport, Transport
LigandIron

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10302-MONOMER
MetaCyc:EG10302-MONOMER

Protein family/group databases

Transport Classification Database

More...TCDBi		1.B.14.1.2 the outer membrane receptor (omr) 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:
Ferrichrome outer membrane transporter/phage receptorCurated
Alternative name(s):
Ferric hydroxamate receptorCurated
Ferric hydroxamate uptakeCurated
Ferrichrome-iron receptor1 Publication
<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:fhuA1 Publication
Synonyms:tonA1 Publication
Ordered Locus Names:b0150, JW0146
<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		EG10302 fhuA

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini34 – 192PeriplasmicAdd BLAST159
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei193 – 201Beta stranded9
Topological domaini202 – 206Extracellular5
Transmembranei207 – 215Beta stranded9
Topological domaini216 – 222Periplasmic7
Transmembranei223 – 231Beta stranded9
Topological domaini232 – 245ExtracellularAdd BLAST14
Transmembranei246 – 255Beta stranded10
Topological domaini256 – 259Periplasmic4
Transmembranei260 – 268Beta stranded9
Topological domaini269 – 312ExtracellularAdd BLAST44
Transmembranei313 – 321Beta stranded9
Topological domaini322 – 326Periplasmic5
Transmembranei327 – 335Beta stranded9
Topological domaini336 – 387ExtracellularAdd BLAST52
Transmembranei388 – 396Beta stranded9
Topological domaini397 – 404Periplasmic8
Transmembranei405 – 413Beta stranded9
Topological domaini414 – 464ExtracellularAdd BLAST51
Transmembranei465 – 473Beta stranded9
Topological domaini474 – 477Periplasmic4
Transmembranei478 – 486Beta stranded9
Topological domaini487 – 508ExtracellularAdd BLAST22
Transmembranei509 – 517Beta stranded9
Topological domaini518 – 522Periplasmic5
Transmembranei523 – 531Beta stranded9
Topological domaini532 – 551ExtracellularAdd BLAST20
Transmembranei552 – 560Beta stranded9
Topological domaini561 – 565Periplasmic5
Transmembranei566 – 574Beta stranded9
Topological domaini575 – 601ExtracellularAdd BLAST27
Transmembranei602 – 610Beta stranded9
Topological domaini611 – 613Periplasmic3
Transmembranei614 – 622Beta stranded9
Topological domaini623 – 645ExtracellularAdd BLAST23
Transmembranei646 – 654Beta stranded9
Topological domaini655 – 661Periplasmic7
Transmembranei662 – 670Beta stranded9
Topological domaini671 – 689ExtracellularAdd BLAST19
Transmembranei690 – 698Beta stranded9
Topological domaini699 – 705Periplasmic7
Transmembranei706 – 714Beta stranded9
Topological domaini715 – 737ExtracellularAdd BLAST23
Transmembranei738 – 746Beta stranded9
Topological domaini747Periplasmic1

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
  • integral component of membrane Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cell outer membrane, Membrane

<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

Chemistry databases

Drug and drug target database

More...DrugBanki		DB02907 2-Amino-Vinyl-Phosphate
DB01814 2-Tridecanoyloxy-Pentadecanoic Acid
DB02700 3-Deoxy-D-Glucosamine
DB03548 3-Deoxy-D-Manno-Oct-2-Ulosonic Acid
DB02767 3-Hydroxy-Myristic Acid
DB04039 3-Oxo-Pentadecanoic Acid
DB02379 Beta-D-Glucose
DB02724 Delta-2-Albomycin A1
DB04160 Diphosphate
DB03574 Ferricrocin-Iron
DB03111 Glucosamine 1-Phosphate
DB02865 Glucosamine 4-Phosphate
DB04526 L-Glycero-D-Manno-Heptopyranose
DB03017 Lauric Acid
DB08231 MYRISTIC ACID
DB02415 N-Octyl-2-Hydroxyethyl Sulfoxide
DB02626 Phenylferricrocin-Iron
DB04220 Rifamycin Cgp 4832

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 331 PublicationAdd BLAST33
<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_000003474834 – 747Ferrichrome outer membrane transporter/phage receptorAdd BLAST714

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi351 ↔ 362
Disulfide bondi725 ↔ 731

Keywords - PTMi

Disulfide bond

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P06971

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

More...PaxDbi		P06971

PRoteomics IDEntifications database

More...PRIDEi		P06971

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P06971

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced 1.6-fold by hydroxyurea.1 Publication

<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

Monomer (PubMed:8916906, PubMed:9856937, PubMed:9865695). Interacts with TonB (PubMed:9353297, PubMed:12427941, PubMed:18653801).6 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

WithEntry#Exp.IntActNotes
mcjAQ9X2V72EBI-1116714,EBI-16100378From Escherichia coli.

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4259745, 139 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2843 Ferrichrome outer membrane transporter complex

Database of interacting proteins

More...DIPi		DIP-9602N

Protein interaction database and analysis system

More...IntActi		P06971, 7 interactors

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_0130

<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

1747
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
1BY3X-ray2.74A34-747[»]
1BY5X-ray2.60A34-747[»]
1FCPX-ray2.70A52-747[»]
1FI1X-ray2.90A52-747[»]
1QFFX-ray2.70A34-747[»]
1QFGX-ray2.50A34-747[»]
1QJQX-ray2.95A34-747[»]
1QKCX-ray3.10A34-747[»]
2FCPX-ray2.50A34-747[»]
2GRXX-ray3.30A/B34-747[»]
4CU4X-ray2.30A53-747[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P06971

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

More...SMRi		P06971

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		P06971

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni148 – 149Ferrichrome binding3 Publications2
Regioni277 – 279Ferrichrome binding3 Publications3
Regioni346 – 348Ferrichrome binding3 Publications3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi40 – 47TonB box8
Motifi730 – 747TonB C-terminal boxAdd BLAST18

<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

Has two distinct conformations in the presence and absence of ferrichrome. The globular N-terminal domain acts a plug that closes the channel formed by the beta-barrel. Binding of ferrichrome at the cell surface induces a conformational change in FhuA, but does not open the channel. Structural changes are propagated and amplified across the plug, and may facilitate binding of FhuA to TonB (PubMed:9865695, PubMed:9353297). TonB binding promotes conformational changes in outer surface-exposed loops of FhuA (PubMed:18653801). Phage T5 is a TonB-independent ligand, and its binding to FhuA results in the formation of high conductance ion channels (PubMed:8617231, PubMed:9353297).4 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 TonB-dependent receptor family.Curated

Keywords - Domaini

Signal, TonB box, Transmembrane, Transmembrane beta strand

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105E0K Bacteria
COG1629 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000260252

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06971

KEGG Orthology (KO)

More...KOi		K02014

Database for complete collections of gene phylogenies

More...PhylomeDBi		P06971

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.170.130.10, 1 hit
2.40.170.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012910 Plug_dom
IPR037066 Plug_dom_sf
IPR039423 TonB-dep_rcpt
IPR000531 TonB-dep_rcpt_b-brl
IPR010916 TonB_box_CS
IPR036942 TonB_rcpt_b-brl_sf
IPR010917 TonB_rcpt_CS
IPR010105 TonB_sidphr_rcpt

The PANTHER Classification System

More...PANTHERi		PTHR32552 PTHR32552, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07715 Plug, 1 hit
PF00593 TonB_dep_Rec, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01783 TonB-siderophor, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00430 TONB_DEPENDENT_REC_1, 1 hit
PS01156 TONB_DEPENDENT_REC_2, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P06971-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARSKTAQPK HSLRKIAVVV ATAVSGMSVY AQAAVEPKED TITVTAAPAP 
        60         70         80         90        100
QESAWGPAAT IAARQSATGT KTDTPIQKVP QSISVVTAEE MALHQPKSVK 
       110        120        130        140        150
EALSYTPGVS VGTRGASNTY DHLIIRGFAA EGQSQNNYLN GLKLQGNFYN 
       160        170        180        190        200
DAVIDPYMLE RAEIMRGPVS VLYGKSSPGG LLNMVSKRPT TEPLKEVQFK 
       210        220        230        240        250
AGTDSLFQTG FDFSDSLDDD GVYSYRLTGL ARSANAQQKG SEEQRYAIAP 
       260        270        280        290        300
AFTWRPDDKT NFTFLSYFQN EPETGYYGWL PKEGTVEPLP NGKRLPTDFN 
       310        320        330        340        350
EGAKNNTYSR NEKMVGYSFD HEFNDTFTVR QNLRFAENKT SQNSVYGYGV 
       360        370        380        390        400
CSDPANAYSK QCAALAPADK GHYLARKYVV DDEKLQNFSV DTQLQSKFAT 
       410        420        430        440        450
GDIDHTLLTG VDFMRMRNDI NAWFGYDDSV PLLNLYNPVN TDFDFNAKDP 
       460        470        480        490        500
ANSGPYRILN KQKQTGVYVQ DQAQWDKVLV TLGGRYDWAD QESLNRVAGT 
       510        520        530        540        550
TDKRDDKQFT WRGGVNYLFD NGVTPYFSYS ESFEPSSQVG KDGNIFAPSK 
       560        570        580        590        600
GKQYEVGVKY VPEDRPIVVT GAVYNLTKTN NLMADPEGSF FSVEGGEIRA 
       610        620        630        640        650
RGVEIEAKAA LSASVNVVGS YTYTDAEYTT DTTYKGNTPA QVPKHMASLW 
       660        670        680        690        700
ADYTFFDGPL SGLTLGTGGR YTGSSYGDPA NSFKVGSYTV VDALVRYDLA 
       710        720        730        740 
RVGMAGSNVA LHVNNLFDRE YVASCFNTYG CFWGAERQVV ATATFRF
Length:747
Mass (Da):82,182
Last modified:November 1, 1997 - v2
<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:i1C2B251D1990E444
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti737R → P in CAA29253 (PubMed:2823072).Curated1

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
M12486 Genomic DNA Translation: AAB61768.1
U00096 Genomic DNA Translation: AAC73261.1
AP009048 Genomic DNA Translation: BAB96726.2
U70214 Genomic DNA Translation: AAB08580.1
X05810 Genomic DNA Translation: CAA29253.1

Protein sequence database of the Protein Information Resource

More...PIRi		F64738 QRECFE

NCBI Reference Sequences

More...RefSeqi		NP_414692.1, NC_000913.3
WP_000124438.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73261; AAC73261; b0150
BAB96726; BAB96726; BAB96726

Database of genes from NCBI RefSeq genomes

More...GeneIDi		944856

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0146
eco:b0150

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2130

<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
M12486 Genomic DNA Translation: AAB61768.1
U00096 Genomic DNA Translation: AAC73261.1
AP009048 Genomic DNA Translation: BAB96726.2
U70214 Genomic DNA Translation: AAB08580.1
X05810 Genomic DNA Translation: CAA29253.1
PIRiF64738 QRECFE
RefSeqiNP_414692.1, NC_000913.3
WP_000124438.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BY3X-ray2.74A34-747[»]
1BY5X-ray2.60A34-747[»]
1FCPX-ray2.70A52-747[»]
1FI1X-ray2.90A52-747[»]
1QFFX-ray2.70A34-747[»]
1QFGX-ray2.50A34-747[»]
1QJQX-ray2.95A34-747[»]
1QKCX-ray3.10A34-747[»]
2FCPX-ray2.50A34-747[»]
2GRXX-ray3.30A/B34-747[»]
4CU4X-ray2.30A53-747[»]
ProteinModelPortaliP06971
SMRiP06971
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259745, 139 interactors
ComplexPortaliCPX-2843 Ferrichrome outer membrane transporter complex
DIPiDIP-9602N
IntActiP06971, 7 interactors
STRINGi316385.ECDH10B_0130

Chemistry databases

DrugBankiDB02907 2-Amino-Vinyl-Phosphate
DB01814 2-Tridecanoyloxy-Pentadecanoic Acid
DB02700 3-Deoxy-D-Glucosamine
DB03548 3-Deoxy-D-Manno-Oct-2-Ulosonic Acid
DB02767 3-Hydroxy-Myristic Acid
DB04039 3-Oxo-Pentadecanoic Acid
DB02379 Beta-D-Glucose
DB02724 Delta-2-Albomycin A1
DB04160 Diphosphate
DB03574 Ferricrocin-Iron
DB03111 Glucosamine 1-Phosphate
DB02865 Glucosamine 4-Phosphate
DB04526 L-Glycero-D-Manno-Heptopyranose
DB03017 Lauric Acid
DB08231 MYRISTIC ACID
DB02415 N-Octyl-2-Hydroxyethyl Sulfoxide
DB02626 Phenylferricrocin-Iron
DB04220 Rifamycin Cgp 4832

Protein family/group databases

TCDBi1.B.14.1.2 the outer membrane receptor (omr) family

PTM databases

CarbonylDBiP06971

Proteomic databases

EPDiP06971
PaxDbiP06971
PRIDEiP06971

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73261; AAC73261; b0150
BAB96726; BAB96726; BAB96726
GeneIDi944856
KEGGiecj:JW0146
eco:b0150
PATRICifig|1411691.4.peg.2130

Organism-specific databases

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

More...EchoBASEi		EB0298
EcoGeneiEG10302 fhuA

Phylogenomic databases

eggNOGiENOG4105E0K Bacteria
COG1629 LUCA
HOGENOMiHOG000260252
InParanoidiP06971
KOiK02014
PhylomeDBiP06971

Enzyme and pathway databases

BioCyciEcoCyc:EG10302-MONOMER
MetaCyc:EG10302-MONOMER

Miscellaneous databases

EvolutionaryTraceiP06971

Protein Ontology

More...PROi		PR:P06971

Family and domain databases

Gene3Di2.170.130.10, 1 hit
2.40.170.20, 1 hit
InterProiView protein in InterPro
IPR012910 Plug_dom
IPR037066 Plug_dom_sf
IPR039423 TonB-dep_rcpt
IPR000531 TonB-dep_rcpt_b-brl
IPR010916 TonB_box_CS
IPR036942 TonB_rcpt_b-brl_sf
IPR010917 TonB_rcpt_CS
IPR010105 TonB_sidphr_rcpt
PANTHERiPTHR32552 PTHR32552, 1 hit
PfamiView protein in Pfam
PF07715 Plug, 1 hit
PF00593 TonB_dep_Rec, 1 hit
TIGRFAMsiTIGR01783 TonB-siderophor, 1 hit
PROSITEiView protein in PROSITE
PS00430 TONB_DEPENDENT_REC_1, 1 hit
PS01156 TONB_DEPENDENT_REC_2, 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 nameiFHUA_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: P06971
Secondary accession number(s): P71280, P75665
<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: November 1, 1997
Last modified: January 16, 2019
This is version 191 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

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