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UniProtKB - P06709 (BIRA_ECOLI)

Entry version 194 (23 Feb 2022)
Sequence version 1 (01 Jan 1988)
Previous versions | rss
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Protein

Bifunctional ligase/repressor BirA

Gene

birA

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

Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.

UniRule annotation4 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

The switch between the enzymatic activity and the repressor activity is regulated by cellular demand for biotin. The switch occurs by swapping of protein interaction partners by holoBirA. In conditions of high biotin demand, holoBirA associates with apoBCCP to transfer biotin. In conditions of low biotin demand, holoBirA dimerizes, binds DNA and represses transcription of the biotin operon.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei112BiotinUniRule annotation2 Publications1
Binding sitei183BiotinUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi22 – 41H-T-H motifUniRule annotationAdd BLAST20

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionDNA-binding, Ligase, Repressor
Biological processTranscription, Transcription regulation
LigandATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:BIOTINLIG-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		6.3.4.15, 2026

Protein family/group databases

MoonProt database of moonlighting proteins

More...MoonProti		P06709

<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:
Bifunctional ligase/repressor BirAUniRule annotation
Alternative name(s):
Biotin operon repressorUniRule annotation
Biotin--[acetyl-CoA-carboxylase] ligaseUniRule annotation (EC:6.3.4.15UniRule annotation)
Biotin--protein ligaseUniRule annotation
Biotin-[acetyl-CoA carboxylase] synthetaseUniRule annotation
<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:birAUniRule annotation
Synonyms:bioR, dhbB
Ordered Locus Names:b3973, JW3941
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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

<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

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>Mutagenesisi52T → I: Does not affect repressor activity. 1 Publication1
Mutagenesisi52T → S: 5-fold increase of repressor activity. Increases binding to DNA. 1 Publication1
Mutagenesisi57G → S: Lack of repressor activity. Does not bind DNA. 1 Publication1
Mutagenesisi58Y → F: Lack of repressor activity. 1 Publication1
Mutagenesisi58Y → T: Does not affect repressor activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3559644

Drug and drug target database

More...DrugBanki		DB04651, BIOTINOL-5-AMP

<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_00000649321 – 321Bifunctional ligase/repressor BirAAdd BLAST321

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P06709

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

More...PaxDbi		P06709

PRoteomics IDEntifications database

More...PRIDEi		P06709

<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 in solution.

Interacts with BCCP. Homodimerizes to bind DNA. Interaction with the corepressor bio-5'-AMP increases dimerization.

6 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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4263391, 269 interactors

Database of interacting proteins

More...DIPi		DIP-9224N

Protein interaction database and analysis system

More...IntActi		P06709, 7 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3973

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P06709

<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

1321
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		P06709

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P06709

<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>Domaini67 – 254BPL/LPL catalyticPROSITE-ProRule annotationAdd BLAST188

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>Regioni89 – 91Biotin binding3
Regioni116 – 118Biotin binding3

<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

Contains an N-terminal helix-turn-helix DNA-binding domain, connected via a linker to the central catalytic domain and the C-terminal domain, which plays roles in dimerization, catalytic function and DNA binding. The N-terminal domain is required for both ligase and repressor activities. It may orient the active site and thereby play an important role in enzymatic activity.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 biotin--protein ligase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0340, Bacteria
COG1654, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_051096_4_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06709

Database for complete collections of gene phylogenies

More...PhylomeDBi		P06709

Family and domain databases

Conserved Domains Database

More...CDDi		cd16442, BPL, 1 hit

Database of protein disorder

More...DisProti		DP00349

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.10, 1 hit
3.30.930.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00978, Bifunct_BirA, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR045864, aa-tRNA-synth_II/BPL/LPL
IPR030855, Bifunct_BirA
IPR004408, Biotin_CoA_COase_ligase
IPR004409, Biotin_operon_repress_HTH
IPR003142, BPL_C
IPR004143, BPL_LPL_catalytic
IPR013196, HTH_11
IPR008988, Transcriptional_repressor_C
IPR036388, WH-like_DNA-bd_sf
IPR036390, WH_DNA-bd_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02237, BPL_C, 1 hit
PF03099, BPL_LplA_LipB, 1 hit
PF08279, HTH_11, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF46785, SSF46785, 1 hit
SSF50037, SSF50037, 1 hit
SSF55681, SSF55681, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00121, birA_ligase, 1 hit
TIGR00122, birA_repr_reg, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51733, BPL_LPL_CATALYTIC, 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.

P06709-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKDNTVPLKL IALLANGEFH SGEQLGETLG MSRAAINKHI QTLRDWGVDV 
        60         70         80         90        100
FTVPGKGYSL PEPIQLLNAK QILGQLDGGS VAVLPVIDST NQYLLDRIGE 
       110        120        130        140        150
LKSGDACIAE YQQAGRGRRG RKWFSPFGAN LYLSMFWRLE QGPAAAIGLS 
       160        170        180        190        200
LVIGIVMAEV LRKLGADKVR VKWPNDLYLQ DRKLAGILVE LTGKTGDAAQ 
       210        220        230        240        250
IVIGAGINMA MRRVEESVVN QGWITLQEAG INLDRNTLAA MLIRELRAAL 
       260        270        280        290        300
ELFEQEGLAP YLSRWEKLDN FINRPVKLII GDKEIFGISR GIDKQGALLL 
       310        320 
EQDGIIKPWM GGEISLRSAE K
Length:321
Mass (Da):35,312
Last modified:January 1, 1988 - 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:iB80AEBCEEE1BD2D4
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti61P → A in strain: RDD012. 1
Natural varianti70K → E in strain: RDD012. 1

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
M10123 Genomic DNA Translation: AAA23520.1
M15820 Genomic DNA Translation: AAA23521.1
L14557 Genomic DNA Translation: AAA24186.1
U00006 Genomic DNA Translation: AAC43075.1
U00096 Genomic DNA Translation: AAC76951.1
AP009048 Genomic DNA Translation: BAE77342.1

Protein sequence database of the Protein Information Resource

More...PIRi		B24029, BVECBF

NCBI Reference Sequences

More...RefSeqi		NP_418404.1, NC_000913.3
WP_000654630.1, NZ_SSZK01000084.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76951; AAC76951; b3973
BAE77342; BAE77342; BAE77342

Database of genes from NCBI RefSeq genomes

More...GeneIDi		58463579
948469

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3941
eco:b3973

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2735

<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
M10123 Genomic DNA Translation: AAA23520.1
M15820 Genomic DNA Translation: AAA23521.1
L14557 Genomic DNA Translation: AAA24186.1
U00006 Genomic DNA Translation: AAC43075.1
U00096 Genomic DNA Translation: AAC76951.1
AP009048 Genomic DNA Translation: BAE77342.1
PIRiB24029, BVECBF
RefSeqiNP_418404.1, NC_000913.3
WP_000654630.1, NZ_SSZK01000084.1

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
1BIAX-ray2.30A1-321[»]
1BIBX-ray2.80A1-321[»]
1HXDX-ray2.40A/B1-321[»]
2EWNX-ray2.80A/B1-321[»]
4WF2X-ray2.31A1-321[»]
SMRiP06709
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263391, 269 interactors
DIPiDIP-9224N
IntActiP06709, 7 interactors
STRINGi511145.b3973

Chemistry databases

BindingDBiP06709
ChEMBLiCHEMBL3559644
DrugBankiDB04651, BIOTINOL-5-AMP

Protein family/group databases

MoonProtiP06709

Proteomic databases

jPOSTiP06709
PaxDbiP06709
PRIDEiP06709

Genome annotation databases

EnsemblBacteriaiAAC76951; AAC76951; b3973
BAE77342; BAE77342; BAE77342
GeneIDi58463579
948469
KEGGiecj:JW3941
eco:b3973
PATRICifig|1411691.4.peg.2735

Organism-specific databases

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

More...EchoBASEi		EB0121

Phylogenomic databases

eggNOGiCOG0340, Bacteria
COG1654, Bacteria
HOGENOMiCLU_051096_4_0_6
InParanoidiP06709
PhylomeDBiP06709

Enzyme and pathway databases

BioCyciEcoCyc:BIOTINLIG-MONOMER
BRENDAi6.3.4.15, 2026

Miscellaneous databases

EvolutionaryTraceiP06709

Protein Ontology

More...PROi		PR:P06709

Family and domain databases

CDDicd16442, BPL, 1 hit
DisProtiDP00349
Gene3Di1.10.10.10, 1 hit
3.30.930.10, 1 hit
HAMAPiMF_00978, Bifunct_BirA, 1 hit
InterProiView protein in InterPro
IPR045864, aa-tRNA-synth_II/BPL/LPL
IPR030855, Bifunct_BirA
IPR004408, Biotin_CoA_COase_ligase
IPR004409, Biotin_operon_repress_HTH
IPR003142, BPL_C
IPR004143, BPL_LPL_catalytic
IPR013196, HTH_11
IPR008988, Transcriptional_repressor_C
IPR036388, WH-like_DNA-bd_sf
IPR036390, WH_DNA-bd_sf
PfamiView protein in Pfam
PF02237, BPL_C, 1 hit
PF03099, BPL_LplA_LipB, 1 hit
PF08279, HTH_11, 1 hit
SUPFAMiSSF46785, SSF46785, 1 hit
SSF50037, SSF50037, 1 hit
SSF55681, SSF55681, 1 hit
TIGRFAMsiTIGR00121, birA_ligase, 1 hit
TIGR00122, birA_repr_reg, 1 hit
PROSITEiView protein in PROSITE
PS51733, BPL_LPL_CATALYTIC, 1 hit

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 nameiBIRA_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: P06709
Secondary accession number(s): Q2M8R4
<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: January 1, 1988
Last sequence update: January 1, 1988
Last modified: February 23, 2022
This is version 194 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, Reference proteome

Documents

  1. UniProtKB entry view manual
    User manual for the UniProtKB entry view
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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