Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P68187 (MALK_ECOLI)

Entry version 146 (18 Sep 2019)
Sequence version 1 (25 Oct 2004)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Maltose/maltodextrin import ATP-binding protein MalK

Gene

malK

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

Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system.2 Publications

Miscellaneous

Target for inducer exclusion, mediated by the unphosphorylated enzyme III of the phosphotransferase system for glucose and resulting in the inhibition of maltose transport.1 Publication
Acts as a repressor of mal genes. In absence of maltose, the C-terminus of MalK interacts with MalT, then MalT becomes inactive and the mal genes are not activated. In presence of maltose, MalK is tightly associated with the MalFG complex and has no affinity for MalT.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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 – 43ATPUniRule 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

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 functionTranslocase
Biological processSugar transport, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:MALK-MONOMER
ECOL316407:JW3995-MONOMER
MetaCyc:MALK-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.6.3.19 2026

Protein family/group databases

MoonProt database of moonlighting proteins

More...MoonProti		P68187

Transport Classification Database

More...TCDBi		3.A.1.1.1 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_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Maltose/maltodextrin import ATP-binding protein MalKUniRule annotation (EC:7.5.2.1UniRule annotation2 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:malK1 PublicationUniRule annotation
Ordered Locus Names:b4035, JW3995
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10558 malK

<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

GO - Cellular componenti

Complete GO annotation on QuickGO ...

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_and_biotech_section">'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>Mutagenesisi85A → M: Suppressor of EAA loop mutations in MalFG. 1 Publication1
Mutagenesisi106K → C: Suppressor of EAA loop mutations in MalFG. 1 Publication1
Mutagenesisi114V → C: Suppressor of EAA loop mutations in MalFG. 1 Publication1
Mutagenesisi117V → M: Suppressor of EAA loop mutations in MalFG. 1 Publication1
Mutagenesisi119E → K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity. 1 Publication1
Mutagenesisi124A → T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity. 1 Publication1
Mutagenesisi137G → A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK. 1 Publication1
Mutagenesisi158D → N: Loss of maltose transport but retains ability to repress mal genes. 1 Publication1
Mutagenesisi228R → C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity. 1 Publication1
Mutagenesisi241F → I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity. 1 Publication1
Mutagenesisi267W → G: Normal maltose transport but constitutive mal gene expression. 1 Publication1
Mutagenesisi278G → P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity. 1 Publication1
Mutagenesisi282S → L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity. 1 Publication1
Mutagenesisi284G → S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity. 1 Publication1
Mutagenesisi302G → D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity. 1 Publication1
Mutagenesisi308E → Q: Maltose transport is affected but retains ability to interact with MalT. 1 Publication1
Mutagenesisi322S → F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity. 1 Publication1
Mutagenesisi340G → A: Maltose transport is affected but retains ability to interact with MalT. 1 Publication1
Mutagenesisi346G → S: Normal maltose transport but constitutive mal gene expression. 1 Publication1
Mutagenesisi355F → Y: Maltose transport is affected but retains ability to interact with MalT. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000924751 – 371Maltose/maltodextrin import ATP-binding protein MalKAdd BLAST371

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P68187

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

More...PaxDbi		P68187

PRoteomics IDEntifications database

More...PRIDEi		P68187

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The complex is composed of two ATP-binding proteins (MalK), two transmembrane proteins (MalG and MalF) and a solute-binding protein (MalE). Protein stability and stable complex formation require YidC.

3 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4262662, 20 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1932 Maltose transport complex
CPX-1978 Enzyme IIA-maltose transporter complex
CPX-2103 MalFGK2 maltose transport complex

Database of interacting proteins

More...DIPi		DIP-47850N

Protein interaction database and analysis system

More...IntActi		P68187, 8 interactors

STRING: functional protein association networks

More...STRINGi		511145.b4035

<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

1371
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		P68187

Database of comparative protein structure models

More...ModBasei		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P68187

<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_and_domains_section">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>Domaini4 – 234ABC transporterUniRule annotationAdd BLAST231

<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. Maltooligosaccharide importer (TC 3.A.1.1.1) family. [View classification]UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4108IJ9 Bacteria
COG3839 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P68187

KEGG Orthology (KO)

More...KOi		K10111

Database for complete collections of gene phylogenies

More...PhylomeDBi		P68187

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003593 AAA+_ATPase
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR015855 ABC_transpr_MalK
IPR008995 Mo/tungstate-bd_C_term_dom
IPR040582 OB_MalK
IPR027417 P-loop_NTPase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00005 ABC_tran, 1 hit
PF17912 OB_MalK, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00382 AAA, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50331 SSF50331, 1 hit
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 1 hit
PS50893 ABC_TRANSPORTER_2, 1 hit
PS51245 MALK, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. 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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P68187-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASVQLQNVT KAWGEVVVSK DINLDIHEGE FVVFVGPSGC GKSTLLRMIA 
        60         70         80         90        100
GLETITSGDL FIGEKRMNDT PPAERGVGMV FQSYALYPHL SVAENMSFGL 
       110        120        130        140        150
KLAGAKKEVI NQRVNQVAEV LQLAHLLDRK PKALSGGQRQ RVAIGRTLVA 
       160        170        180        190        200
EPSVFLLDEP LSNLDAALRV QMRIEISRLH KRLGRTMIYV THDQVEAMTL 
       210        220        230        240        250
ADKIVVLDAG RVAQVGKPLE LYHYPADRFV AGFIGSPKMN FLPVKVTATA 
       260        270        280        290        300
IDQVQVELPM PNRQQVWLPV ESRDVQVGAN MSLGIRPEHL LPSDIADVIL 
       310        320        330        340        350
EGEVQVVEQL GNETQIHIQI PSIRQNLVYR QNDVVLVEEG ATFAIGLPPE 
       360        370 
RCHLFREDGT ACRRLHKEPG V
Length:371
Mass (Da):40,990
Last modified:October 25, 2004 - 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:i240D58F59450F30E
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 CAA23582 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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 conflicti220 – 241ELYHY…PKMNF → AVPLSGRPFCRRIYRFAKDE L in AAB59057 (PubMed:6296778).CuratedAdd BLAST22

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
J01648 Genomic DNA Translation: AAB59057.1
U00006 Genomic DNA Translation: AAC43129.1
U00096 Genomic DNA Translation: AAC77005.1
AP009048 Genomic DNA Translation: BAE78037.1
V00303 Genomic DNA Translation: CAA23582.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...PIRi		B65211 MMECMK

NCBI Reference Sequences

More...RefSeqi		NP_418459.1, NC_000913.3
WP_000179165.1, NZ_STEB01000022.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC77005; AAC77005; b4035
BAE78037; BAE78037; BAE78037

Database of genes from NCBI RefSeq genomes

More...GeneIDi		948537

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3995
eco:b4035

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|511145.12.peg.4150

<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
J01648 Genomic DNA Translation: AAB59057.1
U00006 Genomic DNA Translation: AAC43129.1
U00096 Genomic DNA Translation: AAC77005.1
AP009048 Genomic DNA Translation: BAE78037.1
V00303 Genomic DNA Translation: CAA23582.1 Different initiation.
PIRiB65211 MMECMK
RefSeqiNP_418459.1, NC_000913.3
WP_000179165.1, NZ_STEB01000022.1

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
1Q12X-ray2.60A/B/C/D1-371[»]
1Q1BX-ray2.80A/B/C/D1-371[»]
1Q1EX-ray2.90A/B1-371[»]
2AWNX-ray2.30A/B/C/D1-371[»]
2AWOX-ray2.80A/B/C/D1-371[»]
2R6GX-ray2.80A/B1-371[»]
3FH6X-ray4.50A/B/C/D1-371[»]
3GD7X-ray2.70A/B/C/D219-371[»]
3PUVX-ray2.40A/B1-371[»]
3PUWX-ray2.30A/B1-371[»]
3PUXX-ray2.30A/B1-371[»]
3PUYX-ray3.10A/B1-371[»]
3PUZX-ray2.90A/B1-371[»]
3PV0X-ray3.10A/B1-371[»]
3RLFX-ray2.20A/B1-371[»]
4JBWX-ray3.91A/B/C/D1-371[»]
4KI0X-ray2.38A/B1-371[»]
SMRiP68187
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4262662, 20 interactors
ComplexPortaliCPX-1932 Maltose transport complex
CPX-1978 Enzyme IIA-maltose transporter complex
CPX-2103 MalFGK2 maltose transport complex
DIPiDIP-47850N
IntActiP68187, 8 interactors
STRINGi511145.b4035

Protein family/group databases

MoonProtiP68187
TCDBi3.A.1.1.1 the atp-binding cassette (abc) superfamily

Proteomic databases

jPOSTiP68187
PaxDbiP68187
PRIDEiP68187

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77005; AAC77005; b4035
BAE78037; BAE78037; BAE78037
GeneIDi948537
KEGGiecj:JW3995
eco:b4035
PATRICifig|511145.12.peg.4150

Organism-specific databases

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

More...EchoBASEi		EB0553
EcoGeneiEG10558 malK

Phylogenomic databases

eggNOGiENOG4108IJ9 Bacteria
COG3839 LUCA
InParanoidiP68187
KOiK10111
PhylomeDBiP68187

Enzyme and pathway databases

BioCyciEcoCyc:MALK-MONOMER
ECOL316407:JW3995-MONOMER
MetaCyc:MALK-MONOMER
BRENDAi3.6.3.19 2026

Miscellaneous databases

EvolutionaryTraceiP68187

Protein Ontology

More...PROi		PR:P68187

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR015855 ABC_transpr_MalK
IPR008995 Mo/tungstate-bd_C_term_dom
IPR040582 OB_MalK
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00005 ABC_tran, 1 hit
PF17912 OB_MalK, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF50331 SSF50331, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 1 hit
PS50893 ABC_TRANSPORTER_2, 1 hit
PS51245 MALK, 1 hit

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 nameiMALK_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: P68187
Secondary accession number(s): P02914, Q2M6R9, Q47348
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 25, 2004
Last modified: September 18, 2019
This is version 146 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, Complete proteome, Reference proteome

Documents

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