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Entry version 158 (17 Jun 2020)
Sequence version 2 (01 Nov 1997)
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Protein

ATP-binding protein Uup

Gene

uup

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

Probably plays a role in ribosome assembly or function; overexpression suppresses cold-sensitive growth of a bipA deletion (Ref. 10) (Probable). May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds DNA at Holliday junctions. May be involved in the correct segregation of nucleoids (PubMed:31665437). Has ATPase activity, binds DNA non-sequence specifically; the presence of DNA does not change the ATPase activity (PubMed:16407313). Mutations in this gene cause an increase in RecA-independent precise excision of transposons and insertion elements, and also reduce bacteriophage Mu growth (PubMed:6294054, PubMed:16407313, PubMed:19948254).1 Publication5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

ATPase activity inhibited by N-ethylmaleimide but not by vanadate.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.35 mM for ATP1 Publication
  1. Vmax=26 nmol/min/mg enzyme1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi36 – 43ATP 1UniRule annotation8
Nucleotide bindingi352 – 359ATP 2UniRule annotation8

<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

  • ATPase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: EcoCyc

GO - Biological processi

  • DNA repair Source: UniProtKB-KW
  • regulation of transposon integration Source: EcoCyc
  • response to radiation Source: EcoCyc

<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 functionDNA-binding, Hydrolase
Biological processDNA damage, DNA repair
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:UUP-MONOMER
ECOL316407:JW0932-MONOMER

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.1.120.6 the atp-binding cassette (abc) superfamily

<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%5Fand%5Ftaxonomy%5Fsection">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:
ATP-binding protein UupUniRule annotation (EC:3.6.1.3UniRule annotation1 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:uup1 PublicationUniRule annotation
Synonyms:ycbH, ycbI
Ordered Locus Names:b0949, JW0932
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

<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 UniRule annotation2 Publications
  • Note: Associates with ribosomes.UniRule annotation1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<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

Increase in the frequency of precise transposon excision (PubMed:9139905, PubMed:16407313, PubMed:19948254). No visible growth phenotype at 37 or 18 degrees Celsius. A double bipA-uup deletion does not grow at 18 degrees Celsius, i.e. the uup deletion exacerbates the bipA deletion (Ref. 10). Deletion leads to an increase in DNA crossing over, DNA repeat deletion and DNA repeat expansion; double uup-radD deletion increases the phenotypes. Although single uup deleted cells replicate normally, they are filamentous and lack defined nucleoids, again exacerbated by a radD deletion (PubMed:31665437).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi181D → N: No longer hydrolyzes ATP, has a high level of transposon excision. No growth change at 37 or 18 degrees Celsius, not required to suppress bipA deletion. 2 Publications1
Mutagenesisi182E → Q: Causes growth defect at 37 degrees Celsius, 6-fold decrease in translation; when associated with Q-464 (called EQ2). 1 Publication1
Mutagenesisi294 – 300Missing : Decreases growth at 18 degrees Celsius, does not suppress bipA deletion in cold, stronger association with ribosomes. 1 Publication7
Mutagenesisi465D → N: No longer hydrolyzes ATP, has a high level of transposon excision. Inhibits growth at 37 and 18 degrees Celsius, does not suppress bipA deletion in cold, stronger association with ribosomes. 2 Publications1
Mutagenesisi466E → Q: Causes growth defect at 37 degrees Celsius, 6-fold decrease in translation; when associated with Q-181 (EQ2). 1 Publication1
Mutagenesisi551 – 635Missing : Reduces DNA binding 2-fold, no change in ATP hydrolysis, has a high level of transposon excision. No growth change at 37 or 18 degrees Celsius, does not suppress bipA deletion in cold, stronger association with ribosomes. 3 PublicationsAdd BLAST85

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000930291 – 635ATP-binding protein UupAdd BLAST635

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P43672

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

More...
PaxDbi
P43672

PRoteomics IDEntifications database

More...
PRIDEi
P43672

<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

Present from early exponential to stationary phase in equal amounts (at protein level).2 Publications

<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%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<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
4260026, 20 interactors

Database of interacting proteins

More...
DIPi
DIP-11099N

Protein interaction database and analysis system

More...
IntActi
P43672, 13 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0949

<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

1635
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P43672

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 253ABC transporter 1UniRule annotationAdd BLAST253
Domaini320 – 546ABC transporter 2UniRule annotationAdd BLAST227

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>Regioni551 – 635C-terminal domain (CTD), binds DNA, required to complement a deletion mutant1 PublicationAdd BLAST85

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili563 – 631Combined sources1 PublicationAdd BLAST69

<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

The C-terminal domain (CTD) helps bind DNA, is required to complement a gene deletion.1 Publication

<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 ABC transporter superfamily. ABCF family. Uup subfamily.1 PublicationUniRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C5H Bacteria
COG0488 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000604_36_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P43672

KEGG Orthology (KO)

More...
KOi
K15738

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P43672

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.287.380, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00848 Uup, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR032524 ABC_tran_C
IPR032781 ABC_tran_Xtn
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR027417 P-loop_NTPase
IPR037118 Val-tRNA_synth_C_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00005 ABC_tran, 2 hits
PF16326 ABC_tran_CTD, 1 hit
PF12848 ABC_tran_Xtn, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382 AAA, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 2 hits
PS50893 ABC_TRANSPORTER_2, 2 hits

<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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P43672-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLISMHGAW LSFSDAPLLD NAELHIEDNE RVCLVGRNGA GKSTLMKILN
60 70 80 90 100
REQGLDDGRI IYEQDLIVAR LQQDPPRNVE GSVYDFVAEG IEEQAEYLKR
110 120 130 140 150
YHDISRLVMN DPSEKNLNEL AKVQEQLDHH NLWQLENRIN EVLAQLGLDP
160 170 180 190 200
NVALSSLSGG WLRKAALGRA LVSNPRVLLL DEPTNHLDIE TIDWLEGFLK
210 220 230 240 250
TFNGTIIFIS HDRSFIRNMA TRIVDLDRGK LVTYPGNYDQ YLLEKEEALR
260 270 280 290 300
VEELQNAEFD RKLAQEEVWI RQGIKARRTR NEGRVRALKA MRRERGERRE
310 320 330 340 350
VMGTAKMQVE EASRSGKIVF EMEDVCYQVN GKQLVKDFSA QVLRGDKIAL
360 370 380 390 400
IGPNGCGKTT LLKLMLGQLQ ADSGRIHVGT KLEVAYFDQH RAELDPDKTV
410 420 430 440 450
MDNLAEGKQE VMVNGKPRHV LGYLQDFLFH PKRAMTPVRA LSGGERNRLL
460 470 480 490 500
LARLFLKPSN LLILDEPTND LDVETLELLE ELIDSYQGTV LLVSHDRQFV
510 520 530 540 550
DNTVTECWIF EGGGKIGRYV GGYHDARGQQ EQYVALKQPA VKKTEEAAAA
560 570 580 590 600
KAETVKRSSS KLSYKLQREL EQLPQLLEDL EAKLEALQTQ VADASFFSQP
610 620 630
HEQTQKVLAD MAAAEQELEQ AFERWEYLEA LKNGG
Length:635
Mass (Da):72,067
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:iB1EAC2086BE193D2
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 X81561 differs from that shown. Reason: Frameshift.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC74035.1
AP009048 Genomic DNA Translation: BAA35707.1
Y09439 Genomic DNA Translation: CAA70589.1
X81561 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
D64835

NCBI Reference Sequences

More...
RefSeqi
NP_415469.1, NC_000913.3
WP_000053099.1, NZ_SSZK01000002.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74035; AAC74035; b0949
BAA35707; BAA35707; BAA35707

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945566

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0932
eco:b0949

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1325

<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
U00096 Genomic DNA Translation: AAC74035.1
AP009048 Genomic DNA Translation: BAA35707.1
Y09439 Genomic DNA Translation: CAA70589.1
X81561 Genomic DNA No translation available.
PIRiD64835
RefSeqiNP_415469.1, NC_000913.3
WP_000053099.1, NZ_SSZK01000002.1

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
2LW1NMR-A528-635[»]
SMRiP43672
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260026, 20 interactors
DIPiDIP-11099N
IntActiP43672, 13 interactors
STRINGi511145.b0949

Protein family/group databases

TCDBi3.A.1.120.6 the atp-binding cassette (abc) superfamily

Proteomic databases

jPOSTiP43672
PaxDbiP43672
PRIDEiP43672

Genome annotation databases

EnsemblBacteriaiAAC74035; AAC74035; b0949
BAA35707; BAA35707; BAA35707
GeneIDi945566
KEGGiecj:JW0932
eco:b0949
PATRICifig|1411691.4.peg.1325

Organism-specific databases

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

More...
EchoBASEi
EB2933

Phylogenomic databases

eggNOGiENOG4105C5H Bacteria
COG0488 LUCA
HOGENOMiCLU_000604_36_0_6
InParanoidiP43672
KOiK15738
PhylomeDBiP43672

Enzyme and pathway databases

BioCyciEcoCyc:UUP-MONOMER
ECOL316407:JW0932-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P43672

Family and domain databases

Gene3Di1.10.287.380, 1 hit
HAMAPiMF_00848 Uup, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR032524 ABC_tran_C
IPR032781 ABC_tran_Xtn
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR027417 P-loop_NTPase
IPR037118 Val-tRNA_synth_C_sf
PfamiView protein in Pfam
PF00005 ABC_tran, 2 hits
PF16326 ABC_tran_CTD, 1 hit
PF12848 ABC_tran_Xtn, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 2 hits
SUPFAMiSSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 2 hits
PS50893 ABC_TRANSPORTER_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiUUP_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: P43672
Secondary accession number(s): O05662, P43673, P75865
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: June 17, 2020
This is version 158 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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