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Entry version 6 (02 Dec 2020)
Sequence version 1 (26 Feb 2020)
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Protein

50S ribosomal subunit assembly factor BipA

Gene

bipA

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

A 50S ribosomal subunit assembly protein with GTPase and nucleotide-independent chaperone activity, required for 50S subunit assembly at low temperatures, may also play a role in translation (PubMed:30305394). Genetic and deletion evidence suggests this is involved in ribosome assembly at low temperatures; it may also affect translation (Probable) (PubMed:25777676, PubMed:30305394). Involved in incorporation of ribosomal protein L6 into precursor 44S ribosomal particles at low temperatures. Also has chaperone activity which does not require nucleotides (PubMed:30305394). Binds GDP, ppGpp and GDPCP (a nonhydrolyzable GTP analog) with similar affinity; the conformation of the protein does not significantly change upon nucleotide binding (PubMed:26163516, PubMed:26283392). Interacts with ribosomes (Ref. 12, PubMed:26283392). Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA. Ribosome binding alters its conformation (PubMed:26283392). Genetically its function does not overlap LepA, and it acts in a different pathway during ribosome assembly than does RNA helicase DeaD (PubMed:25777676). GTPase that affects interactions between enteropathogenic E.coli (EPEC) and epithelial cells (PubMed:9622352). Probably regulates expression of proteins required for (at least) K5 polysaccharide production (Probable). Deletion mutants of bipA are suppressed by an rluC deletion, which no longer modifies uracils 955, 2504 and 2580 to pseudouridine in 23S rRNA; there are 5 other pseudouridine synthases in E.coli, only rluC suppresses this phenotype. Mutating 23S rRNA so the 3 uracils are other nucleotides also suppresses the bipA deletion; pseudouridine-2504 is required for ribosome assembly and translational accuracy (PubMed:18820021, PubMed:25777676).2 Publications7 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

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 bindingi15 – 20GTPUniRule annotationCombined sources2 Publications6
Nucleotide bindingi128 – 131GTPUniRule annotationCombined sources1 Publication4
Nucleotide bindingi166 – 168GTPCombined sources1 Publication3

<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

GO - Biological processi

<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 functionChaperone, Hydrolase, RNA-binding, rRNA-binding, tRNA-binding
Biological processRibosome biogenesis
LigandGTP-binding, Nucleotide-binding

<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:
50S ribosomal subunit assembly factor BipA1 PublicationUniRule annotation (EC:3.6.5.-UniRule annotation1 Publication)
Alternative name(s):
GTP-binding protein BipA/TypA
Ribosome assembly factor BipA
Ribosome-dependent GTPase BipA
Tyrosine phosphorylated protein A
<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:bipA1 PublicationUniRule annotation
Synonyms:o5911 Publication, typA, yihK
Ordered Locus Names:b3871, JW5571
<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 70S ribosomes and 30S and 50S subunits in the presence of GMPPNP (a nonhydrolyzable GTP analog) at both 20 and 37 degrees Celsius; no change in ribosome association is seen in the presence of ppGpp or when the stringent response is triggered.1 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

Decreased extracellular K5 polysaccharide production at 37 degrees Celsius, increased extracellular K5 polysaccharide production at 20 degrees Celsius (PubMed:10781541). Cold-sensitive growth (20 degrees Celsius); cells have a long lag phase and double more slowly (PubMed:11683274, PubMed:18820021). Decreased capsule synthesis. Cold sensitive growth and decreased capsule synthesis are suppressed by an rluC deletion (PubMed:18820021). Cold-sensitive growth (20 degrees Celsius); a single bipA deletion has a disturbed ribosome profile at low temperature, with more 30S than 50S subunits, accumulation of a precursor-23S rRNA and precursor 50S subunit and decreased 70S ribosomes (PubMed:25777676, PubMed:30305394). These ribosome phenotypes are suppressed in an rluC deletion. A double bipA-deaD deletion has a more severe growth and ribosome phenotype than either single deletion (PubMed:25777676). At 20 degrees Celsius the single deletion is missing ribosomal protein L6 and has decreased amounts of L9 and L18 and makes less capsule. It has decreased motility at both 20 and 37 degrees Celsius (PubMed:30305394). Cold-sensitive growth (18 degrees Celsius); 2-fold more Uup is expressed at 37 degrees Celsius, 10-fold more Uup at 18 degrees Celsius. A double bipA-uup deletion does not grow at 18 degrees Celsius (Ref. 12).6 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>Mutagenesisi128N → D: No GTPase activity, does not restore normal ribosomes to a bipA deletion, does not associate with ribosomes, retains its ability to help proteins refold. 1 Publication1
Mutagenesisi164Y → P: No change in growth at 20 degrees Celsius. 1 Publication1
Mutagenesisi472Y → P: No change in growth at 20 degrees Celsius. 1 Publication1
Mutagenesisi519Y → P: No change in growth at 20 degrees Celsius. 1 Publication1

<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_00000915501 – 60750S ribosomal subunit assembly factor BipAAdd BLAST607

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Very poorly to not phosphorylated on tyrosine (PubMed:9622352, PubMed:9642082, PubMed:30305394). Phosphorylation in vitro is strongly activated by proteins present in pathogenic strain E2348/69 / EPEC / MAR001 but not non-pathogenic strain K12 / DH5 alpha. Phosphorylation in vitro increases GTPase activity (PubMed:9622352). Mutation of 3 conserved Tyr residues (Tyr-164; Ty5-47 or Tyr-591) to Phe alone or in all combinations has no effect on the ability of the protein to restore growth to a deletion mutant, suggesting Tyr-phosphorylation is not important in non-EPEC strains (PubMed:30305394).3 Publications

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0DTT0

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

More...
PaxDbi
P32132

<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 about 2-fold at 18 degrees Celsius (at protein level) (Ref. 12). Basally expressed at 37 degrees Celsius, 3.5-fold induced after shift to 20 degrees Celsius, maximal expression is seen at 2 hours (at protein level). No increase in expression when cells are grown at 43 degrees Celsius or when engineered to produce increased levels of the stress second messenger ppGpp. Expression at low temperatures is activated by CRP (PubMed:30305394).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">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:26163516, PubMed:26283392). Binds between the 30S and 50S ribosomal subunits, in a similar position as ribosome-bound EF-G; it contacts proteins L7/12, L11, S2, 16S and 23S rRNA and the A-site tRNA. Binding to the ribosome alters its conformation (PubMed:26283392).

2 Publications

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

Hide details

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-11058N

Protein interaction database and analysis system

More...
IntActi
P0DTT0, 5 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3871

<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

1607
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
P0DTT0

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>Domaini3 – 198tr-type GUniRule annotationAdd BLAST196

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>Regioni1 – 202Domain I (or G domain), required for chaperone activity2 Publications1 PublicationAdd BLAST202
Regioni203 – 320Domain II (or beta barrel domain)2 PublicationsAdd BLAST118
Regioni303 – 385Domain III2 PublicationsAdd BLAST83
Regioni386 – 482Domain V2 PublicationsAdd BLAST97
Regioni483 – 607C-terminal domain (CTD), binds A-site tRNA2 PublicationsAdd BLAST125

<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

Crystallizes with 2 superdomains; the first comprises domains I (residues 1-202, also called the G domain) and II (203-302, also called the beta barrel domain), while the second is composed of domains III (303-385), V (386-482) and a BipA-specific C-terminal domain (CTD, 483-607). Domains I-V are homologous to domains in EF-G and LepA; although the domains are similar, their relative arrangement is different (PubMed:26163516, PubMed:26283392). The structure of isolated superdomain 2 is more compact in the presence of Mg2+ than in the intact protein (PubMed:26163516). Upon ribosome binding the second superdomain shifts and the CTD assumes a more compact conformation. The CTD binds to the A-site tRNA (PubMed:26283392). Chaperone activity resides in domain I; truncated proteins of 49-607 and 149-607 have no chaperone activity (PubMed:30305394).3 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

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32132

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P32132

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03710, BipA_TypA_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.40.50.250, 1 hit

HAMAP database of protein families

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HAMAPi
MF_00849, BipA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035651, BipA_V
IPR035647, EFG_III/V
IPR000640, EFG_V-like
IPR004161, EFTu-like_2
IPR031157, G_TR_CS
IPR027417, P-loop_NTPase
IPR005225, Small_GTP-bd_dom
IPR000795, TF_GTP-bd_dom
IPR009000, Transl_B-barrel_sf
IPR042116, TypA/BipA_C
IPR006298, TypA_GTP-bd

The PANTHER Classification System

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PANTHERi
PTHR42908:SF8, PTHR42908:SF8, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00679, EFG_C, 1 hit
PF00009, GTP_EFTU, 1 hit
PF03144, GTP_EFTU_D2, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00315, ELONGATNFCT

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50447, SSF50447, 1 hit
SSF52540, SSF52540, 1 hit
SSF54980, SSF54980, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00231, small_GTP, 1 hit
TIGR01394, TypA_BipA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00301, G_TR_1, 1 hit
PS51722, G_TR_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%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.

P0DTT0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIEKLRNIAI IAHVDHGKTT LVDKLLQQSG TFDSRAETQE RVMDSNDLEK
60 70 80 90 100
ERGITILAKN TAIKWNDYRI NIVDTPGHAD FGGEVERVMS MVDSVLLVVD
110 120 130 140 150
AFDGPMPQTR FVTKKAFAYG LKPIVVINKV DRPGARPDWV VDQVFDLFVN
160 170 180 190 200
LDATDEQLDF PIVYASALNG IAGLDHEDMA EDMTPLYQAI VDHVPAPDVD
210 220 230 240 250
LDGPFQMQIS QLDYNSYVGV IGIGRIKRGK VKPNQQVTII DSEGKTRNAK
260 270 280 290 300
VGKVLGHLGL ERIETDLAEA GDIVAITGLG ELNISDTVCD TQNVEALPAL
310 320 330 340 350
SVDEPTVSMF FCVNTSPFCG KEGKFVTSRQ ILDRLNKELV HNVALRVEET
360 370 380 390 400
EDADAFRVSG RGELHLSVLI ENMRREGFEL AVSRPKVIFR EIDGRKQEPY
410 420 430 440 450
ENVTLDVEEQ HQGSVMQALG ERKGDLKNMN PDGKGRVRLD YVIPSRGLIG
460 470 480 490 500
FRSEFMTMTS GTGLLYSTFS HYDDVRPGEV GQRQNGVLIS NGQGKAVAFA
510 520 530 540 550
LFGLQDRGKL FLGHGAEVYE GQIIGIHSRS NDLTVNCLTG KKLTNMRASG
560 570 580 590 600
TDEAVVLVPP IRMTLEQALE FIDDDELVEV TPTSIRIRKR HLTENDRRRA

NRAPKDD
Length:607
Mass (Da):67,355
Last modified:February 26, 2020 - 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:i3B4DE3A514F95FFB
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 conflicti592 – 607Missing in AAB03005 (PubMed:8346018).CuratedAdd BLAST16

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
L19201 Genomic DNA Translation: AAB03005.1
U00096 Genomic DNA Translation: AAT48232.1
AP009048 Genomic DNA Translation: BAE77438.1

Protein sequence database of the Protein Information Resource

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PIRi
S40816

NCBI Reference Sequences

More...
RefSeqi
WP_000570668.1, NZ_STEB01000017.1
YP_026274.1, NC_000913.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
49586844
948369

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW5571
eco:b3871

Pathosystems Resource Integration Center (PATRIC)

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PATRICi
fig|1411691.4.peg.2840

<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
L19201 Genomic DNA Translation: AAB03005.1
U00096 Genomic DNA Translation: AAT48232.1
AP009048 Genomic DNA Translation: BAE77438.1
PIRiS40816
RefSeqiWP_000570668.1, NZ_STEB01000017.1
YP_026274.1, NC_000913.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZCIX-ray2.63A/B1-601[»]
4ZCKX-ray2.48A306-603[»]
4ZCLX-ray3.06A/B1-601[»]
4ZCMX-ray3.31A/B1-607[»]
5A9VX-ray3.31A/B/C/D/E/F1-607[»]
5A9WX-ray3.70A1-607[»]
5A9XX-ray3.80A1-607[»]
5A9YX-ray4.00A1-607[»]
5A9Zelectron microscopy4.70CA1-605[»]
5AA0electron microscopy5.00BZ1-605[»]
SMRiP0DTT0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-11058N
IntActiP0DTT0, 5 interactors
STRINGi511145.b3871

Proteomic databases

jPOSTiP0DTT0
PaxDbiP32132

Genome annotation databases

GeneIDi49586844
948369
KEGGiecj:JW5571
eco:b3871
PATRICifig|1411691.4.peg.2840

Organism-specific databases

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

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EchoBASEi
EB1783

Phylogenomic databases

InParanoidiP32132
PhylomeDBiP32132

Miscellaneous databases

Protein Ontology

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PROi
PR:P32132

Family and domain databases

CDDicd03710, BipA_TypA_C, 1 hit
Gene3Di2.40.50.250, 1 hit
HAMAPiMF_00849, BipA, 1 hit
InterProiView protein in InterPro
IPR035651, BipA_V
IPR035647, EFG_III/V
IPR000640, EFG_V-like
IPR004161, EFTu-like_2
IPR031157, G_TR_CS
IPR027417, P-loop_NTPase
IPR005225, Small_GTP-bd_dom
IPR000795, TF_GTP-bd_dom
IPR009000, Transl_B-barrel_sf
IPR042116, TypA/BipA_C
IPR006298, TypA_GTP-bd
PANTHERiPTHR42908:SF8, PTHR42908:SF8, 1 hit
PfamiView protein in Pfam
PF00679, EFG_C, 1 hit
PF00009, GTP_EFTU, 1 hit
PF03144, GTP_EFTU_D2, 1 hit
PRINTSiPR00315, ELONGATNFCT
SUPFAMiSSF50447, SSF50447, 1 hit
SSF52540, SSF52540, 1 hit
SSF54980, SSF54980, 2 hits
TIGRFAMsiTIGR00231, small_GTP, 1 hit
TIGR01394, TypA_BipA, 1 hit
PROSITEiView protein in PROSITE
PS00301, G_TR_1, 1 hit
PS51722, G_TR_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiBIPA_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: P0DTT0
Secondary accession number(s): P32132, Q2M8G8, Q6BEY2
<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: February 26, 2020
Last sequence update: February 26, 2020
Last modified: December 2, 2020
This is version 6 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, 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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