Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 139 (02 Jun 2021)
Sequence version 1 (01 Aug 1998)
Previous versions | rss
Add a publicationFeedback
Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Aquifex aeolicus (strain VF5)
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

Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.

UniRule annotation3 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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotation3 Publications, Mn2+1 Publication

<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

Inhibited by natural nucleoside antibiotics including tunicamycin, capuramycin and muraymycin. Usually the cofactor magnesium is not required for antibiotic binding.3 Publications

<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=190 µM for UDP-MurNAc-pentapeptide1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: peptidoglycan biosynthesis

    This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

    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 sitei70InhibitorCombined sources1 Publication1
    Binding sitei75InhibitorCombined sources1 Publication1
    Binding sitei190InhibitorCombined sources1 Publication1
    Binding sitei193InhibitorCombined sources1 Publication1
    Binding sitei196InhibitorCombined sources1 Publication1
    Binding sitei264Inhibitor; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
    Binding sitei268InhibitorCombined sources1 Publication1
    Binding sitei305InhibitorCombined sources1 Publication1
    Binding sitei321Inhibitor; via carbonyl oxygenCombined sources1 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

    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 functionTransferase
    Biological processCell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
    LigandMagnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    AAEO224324:G1G15-40-MONOMER

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00219

    <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:
    Phospho-N-acetylmuramoyl-pentapeptide-transferaseUniRule annotation (EC:2.7.8.13UniRule annotation3 Publications)
    Alternative name(s):
    UDP-MurNAc-pentapeptide phosphotransferaseUniRule 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:mraYUniRule annotation
    Ordered Locus Names:aq_053
    <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>OrganismiAquifex aeolicus (strain VF5)
    <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 identifieri224324 [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 lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
    <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
    • UP000000798 <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

    <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%5Flocation%5Fsection">'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 domaini1 – 25Periplasmic1 PublicationAdd BLAST25
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei26 – 48Helical; Name=Helix 11 PublicationAdd BLAST23
    Topological domaini49 – 74Cytoplasmic1 PublicationAdd BLAST26
    Transmembranei75 – 92Helical; Name=Helix 21 PublicationAdd BLAST18
    Topological domaini93 – 98Periplasmic1 Publication6
    Transmembranei99 – 120Helical; Name=Helix 31 PublicationAdd BLAST22
    Topological domaini121 – 130Cytoplasmic1 Publication10
    Transmembranei131 – 152Helical; Name=Helix 41 PublicationAdd BLAST22
    Topological domaini153 – 172Periplasmic1 PublicationAdd BLAST20
    Transmembranei173 – 194Helical; Name=Helix 51 PublicationAdd BLAST22
    Topological domaini195 – 197Cytoplasmic1 Publication3
    Transmembranei198 – 218Helical; Name=Helix 61 PublicationAdd BLAST21
    Topological domaini219 – 233Periplasmic1 PublicationAdd BLAST15
    Transmembranei234 – 255Helical; Name=Helix 71 PublicationAdd BLAST22
    Topological domaini256 – 264Cytoplasmic1 Publication9
    Transmembranei265 – 280Helical; Name=Helix 81 PublicationAdd BLAST16
    Topological domaini281 – 284Periplasmic1 Publication4
    Transmembranei285 – 310Helical; Name=Helix 91 PublicationAdd BLAST26
    Topological domaini311 – 332Cytoplasmic1 PublicationAdd BLAST22
    Transmembranei333 – 355Helical; Name=Helix 101 PublicationAdd BLAST23
    Topological domaini356 – 359Periplasmic1 Publication4

    Keywords - Cellular componenti

    Cell inner membrane, Cell 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

    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>Mutagenesisi70K → A: Reduces binding to inhibitor. 1 Publication1
    Mutagenesisi117D → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi118D → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi190N → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi193D → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi196D → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi196D → N: Loss of catalytic activity. 1 Publication1
    Mutagenesisi262F → A: Impairs binding to inhibitor. 1 Publication1
    Mutagenesisi262F → W: Reduces binding to inhibitor. 1 Publication1
    Mutagenesisi265D → A: Loss of catalytic activity. Reduces binding to inhibitor. 2 Publications1
    Mutagenesisi305Q → A: Impairs binding to inhibitor. 1 Publication1
    Mutagenesisi324H → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi325H → A: Reduces the catalytic activity. 1 Publication1
    Mutagenesisi326H → A: Reduces the catalytic activity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4295560

    <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_00001087721 – 359Phospho-N-acetylmuramoyl-pentapeptide-transferaseAdd BLAST359

    <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

    Homodimer.

    1 Publication

    <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

    O66465
    With#Exp.IntAct
    itself5EBI-16071899,EBI-16071899

    GO - Molecular functioni

    Protein-protein interaction databases

    Database of interacting proteins

    More...
    DIPi
    DIP-61734N

    STRING: functional protein association networks

    More...
    STRINGi
    224324.aq_053

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    O66465

    <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

    1359
    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
    O66465

    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

    <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 glycosyltransferase 4 family. MraY subfamily.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0472, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_023982_0_0_0

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    O66465

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    LMSPLHH

    Database of Orthologous Groups

    More...
    OrthoDBi
    1151822at2

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd06852, GT_MraY, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00038, MraY, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000715, Glycosyl_transferase_4
    IPR003524, PNAcMuramoyl-5peptid_Trfase
    IPR018480, PNAcMuramoyl-5peptid_Trfase_CS

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR22926, PTHR22926, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00953, Glycos_transf_4, 1 hit
    PF10555, MraY_sig1, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00445, mraY, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01347, MRAY_1, 1 hit
    PS01348, MRAY_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.

    O66465-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLYQLALLLK DYWFAFNVLK YITFRSFTAV LIAFFLTLVL SPSFINRLRK
    60 70 80 90 100
    IQRLFGGYVR EYTPESHEVK KYTPTMGGIV ILIVVTLSTL LLMRWDIKYT
    110 120 130 140 150
    WVVLLSFLSF GTIGFWDDYV KLKNKKGISI KTKFLLQVLS ASLISVLIYY
    160 170 180 190 200
    WADIDTILYF PFFKELYVDL GVLYLPFAVF VIVGSANAVN LTDGLDGLAI
    210 220 230 240 250
    GPAMTTATAL GVVAYAVGHS KIAQYLNIPY VPYAGELTVF CFALVGAGLG
    260 270 280 290 300
    FLWFNSFPAQ MFMGDVGSLS IGASLATVAL LTKSEFIFAV AAGVFVFETI
    310 320 330 340 350
    SVILQIIYFR WTGGKRLFKR APFHHHLELN GLPEPKIVVR MWIISILLAI

    IAISMLKLR
    Length:359
    Mass (Da):40,341
    Last modified:August 1, 1998 - 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:iB2D6292EA6EA16D4
    GO

    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
    AE000657 Genomic DNA Translation: AAC06418.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    F70304

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_213025.1, NC_000918.1
    WP_010879963.1, NC_000918.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC06418; AAC06418; aq_053

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    aae:aq_053

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|224324.8.peg.41

    <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
    AE000657 Genomic DNA Translation: AAC06418.1
    PIRiF70304
    RefSeqiNP_213025.1, NC_000918.1
    WP_010879963.1, NC_000918.1

    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
    4J72X-ray3.30A/B1-359[»]
    5CKRX-ray2.95A1-359[»]
    6OYHX-ray2.95A/B/C/D1-359[»]
    6OYZX-ray3.62A/B/C/D1-359[»]
    6OZ6X-ray3.70A/B/C/D1-359[»]
    SMRiO66465
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    DIPiDIP-61734N
    STRINGi224324.aq_053

    Chemistry databases

    BindingDBiO66465
    ChEMBLiCHEMBL4295560

    Protocols and materials databases

    ABCD curated depository of sequenced antibodies

    More...
    ABCDi
    O66465, 1 sequenced antibody

    Genome annotation databases

    EnsemblBacteriaiAAC06418; AAC06418; aq_053
    KEGGiaae:aq_053
    PATRICifig|224324.8.peg.41

    Phylogenomic databases

    eggNOGiCOG0472, Bacteria
    HOGENOMiCLU_023982_0_0_0
    InParanoidiO66465
    OMAiLMSPLHH
    OrthoDBi1151822at2

    Enzyme and pathway databases

    UniPathwayiUPA00219
    BioCyciAAEO224324:G1G15-40-MONOMER

    Family and domain databases

    CDDicd06852, GT_MraY, 1 hit
    HAMAPiMF_00038, MraY, 1 hit
    InterProiView protein in InterPro
    IPR000715, Glycosyl_transferase_4
    IPR003524, PNAcMuramoyl-5peptid_Trfase
    IPR018480, PNAcMuramoyl-5peptid_Trfase_CS
    PANTHERiPTHR22926, PTHR22926, 1 hit
    PfamiView protein in Pfam
    PF00953, Glycos_transf_4, 1 hit
    PF10555, MraY_sig1, 1 hit
    TIGRFAMsiTIGR00445, mraY, 1 hit
    PROSITEiView protein in PROSITE
    PS01347, MRAY_1, 1 hit
    PS01348, MRAY_2, 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 nameiMRAY_AQUAE
    <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: O66465
    <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: May 30, 2000
    Last sequence update: August 1, 1998
    Last modified: June 2, 2021
    This is version 139 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again