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UniProtKB - P02943 (LAMB_ECOLI)

Entry version 200 (02 Jun 2021)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
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Protein

Maltoporin

Gene

lamB

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

Involved in the transport of maltose and maltodextrins (PubMed:3301537, PubMed:2832377, PubMed:11742115, PubMed:7824948, PubMed:8805519, PubMed:9299337).

Indispensable for translocation of maltodextrins (alpha 1-4 linked polyglucosyls) containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel (PubMed:7824948, PubMed:8805519, PubMed:9299337, PubMed:11742115).

Also acts as a receptor for several bacteriophages including lambda (PubMed:4201774).

Binds maltosaccharides; when LamB binds starch in soft agar, it inhibits motility (PubMed:2832377).

7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei31Greasy slide, important in sugar transportUniRule annotation2 Publications1
Sitei66Greasy slide, important in sugar transportUniRule annotation2 Publications1
Sitei99Greasy slide, important in sugar transportUniRule annotation2 Publications1
Sitei143Important in sugar transportUniRule annotation1 Publication1
Sitei252Greasy slide, important in sugar transportUniRule annotation2 Publications1
Sitei383Greasy slide, important in sugar transportUniRule annotation2 Publications1
Sitei445Greasy slide, important in sugar transportUniRule annotation2 Publications1

<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 functionHost cell receptor for virus entry, Porin, Receptor
Biological processHost-virus interaction, Ion transport, Sugar transport, Transport

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10528-MONOMER
MetaCyc:EG10528-MONOMER

Protein family/group databases

Transport Classification Database

More...TCDBi		1.B.3.1.1, the sugar porin (sp) family

<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:
MaltoporinUniRule annotation
Alternative name(s):
Maltose outer membrane channelCurated
Maltose-inducible porinUniRule annotation
Phage lambda receptor protein1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:lamBUniRule annotation
Synonyms:malB
Ordered Locus Names:b4036, JW3996
<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

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 domaini26Periplasmic1
<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>Transmembranei27 – 40Beta strandedAdd BLAST14
Topological domaini41 – 64Extracellular1 PublicationAdd BLAST24
Transmembranei65 – 75Beta strandedAdd BLAST11
Topological domaini76 – 81Periplasmic1 Publication6
Transmembranei82 – 93Beta strandedAdd BLAST12
Topological domaini94 – 104Extracellular1 PublicationAdd BLAST11
Transmembranei105 – 115Beta strandedAdd BLAST11
Topological domaini116 – 122Periplasmic1 Publication7
Transmembranei123 – 130Beta stranded8
Topological domaini131 – 156Extracellular1 PublicationAdd BLAST26
Transmembranei157 – 159Beta stranded3
Topological domaini160 – 161Periplasmic1 Publication2
Transmembranei162 – 173Beta strandedAdd BLAST12
Topological domaini174 – 191Extracellular1 PublicationAdd BLAST18
Transmembranei192 – 204Beta strandedAdd BLAST13
Topological domaini205 – 208Periplasmic1 Publication4
Transmembranei209 – 222Beta strandedAdd BLAST14
Topological domaini223 – 234Extracellular1 PublicationAdd BLAST12
Transmembranei235 – 248Beta strandedAdd BLAST14
Topological domaini249 – 250Periplasmic1 Publication2
Transmembranei251 – 263Beta strandedAdd BLAST13
Topological domaini264 – 290Extracellular1 PublicationAdd BLAST27
Transmembranei291 – 305Beta strandedAdd BLAST15
Topological domaini306 – 307Periplasmic1 Publication2
Transmembranei308 – 323Beta strandedAdd BLAST16
Topological domaini324 – 326Extracellular1 Publication3
Transmembranei327 – 341Beta strandedAdd BLAST15
Topological domaini342 – 344Periplasmic1 Publication3
Transmembranei345 – 359Beta strandedAdd BLAST15
Topological domaini360 – 362Extracellular1 Publication3
Transmembranei363 – 376Beta strandedAdd BLAST14
Topological domaini377 – 386Periplasmic1 Publication10
Transmembranei387 – 399Beta strandedAdd BLAST13
Topological domaini400 – 430Extracellular1 PublicationAdd BLAST31
Transmembranei431 – 445Beta strandedAdd BLAST15
Topological domaini446Periplasmic1

Keywords - Cellular componenti

Cell outer 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

<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

Resistance to phage lambda (PubMed:4201774). No growth on dextrins (PubMed:2832377).2 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>Mutagenesisi33R → H in lamB1040; reduces ligand affinity and pore size, no longer selective for maltodextrins. Reduced starch binding, grows on maltodextrins, no change in phage lambda binding. 2 Publications1
Mutagenesisi34S → SGS in lamB375; decreased protein at 37 but not 30 degrees Celsius, reduced starch binding, no growth on dextrins, decreased affinity for maltose, loss of phage lambda binding. 1 Publication1
Mutagenesisi47C → S: Normal transport activity, assembled trimer is less stable. 1 Publication1
Mutagenesisi63C → S: Normal transport activity, assembled trimer is less stable. 1 Publication1
Mutagenesisi99W → R: Decreases starch affinity, slightly increases maltose affinity. 1 Publication1
Mutagenesisi104P → PDP in lamB147; decreased affinity for maltose, grows on maltodextrins, no change in phage lambda binding. 1 Publication1
Mutagenesisi107R → S: Decreases maltodextrin affinity, increases sucrose binding and transport. 1 Publication1
Mutagenesisi134R → A: Considerable increase in pore size and sucrose transport, slight decrease in maltose transport; when associated with A-143. 1 Publication1
Mutagenesisi134R → D or N: Slight increase in pore size; increase in sucrose transport and slight decrease in maltose transport; when associated with D-143 and F-146. 1 Publication1
Mutagenesisi143Y → F: Increases affinity for starch and maltose, pore size and transport of maltohexaose. 2 Publications1
Mutagenesisi143Y → YY in lamB203; reduced starch binding, no maltose transport, no growth on dextrins, decreased protein in outer membrane at 37 but not 30 degrees Celsius, no change in phage lambda binding. 1 Publication1
Mutagenesisi146D → G: Increases affinity for large dextrins. 2 Publications1
Mutagenesisi219G → D in lamB1002; decreased affinity for maltose, loss of phage lambda binding. 1 Publication1
Mutagenesisi385R → C in lamb1004; reduced starch binding, decreased affinity for maltose, no change in phage lambda binding. 1 Publication1
Mutagenesisi386P → PDP in lamB146; loss of starch binding, grows poorly on maltodextrins, reduced affinity for somaltose. 1 Publication1
Mutagenesisi445 – 446Missing in lamB1007; significantly less protein in outer membrane, no growth on dextrins, reduced susceptibility to phage lambda. 1 Publication2

Chemistry databases

Drug and drug target database

More...DrugBanki		DB02379, Beta-D-Glucose
DB04173, Fructose

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 251 PublicationAdd BLAST25
<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_000002517526 – 446MaltoporinUniRule annotationAdd BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi47 ↔ 631 Publication1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P02943

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

More...PaxDbi		P02943

PRoteomics IDEntifications database

More...PRIDEi		P02943

<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

By maltose.UniRule annotation1 Publication

<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

Homotrimer formed of three 18-stranded antiparallel beta-barrels, containing three independent channels (PubMed:1988451, PubMed:16079137, PubMed:7824948, PubMed:8805519, PubMed:9299337) (By similarity). An intrasubunit disulfide bond contributes to trimer stability (PubMed:1988451).

UniRule annotation5 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4262663, 259 interactors

Database of interacting proteins

More...DIPi		DIP-10082N

Protein interaction database and analysis system

More...IntActi		P02943, 3 interactors

STRING: functional protein association networks

More...STRINGi		511145.b4036

<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

1446
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		P02943

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		P02943

<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 porin LamB (TC 1.B.3) family. [View classification]UniRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG4580, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_032473_4_1_6

Family and domain databases

Conserved Domains Database

More...CDDi		cd01346, Maltoporin-like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.170.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01301, LamB, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR023738, Maltoporin
IPR003192, Porin_LamB
IPR036998, Porin_LamB_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02264, LamB, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P02943-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMITLRKLPL AVAVAAGVMS AQAMAVDFHG YARSGIGWTG SGGEQQCFQT 
        60         70         80         90        100
TGAQSKYRLG NECETYAELK LGQEVWKEGD KSFYFDTNVA YSVAQQNDWE 
       110        120        130        140        150
ATDPAFREAN VQGKNLIEWL PGSTIWAGKR FYQRHDVHMI DFYYWDISGP 
       160        170        180        190        200
GAGLENIDVG FGKLSLAATR SSEAGGSSSF ASNNIYDYTN ETANDVFDVR 
       210        220        230        240        250
LAQMEINPGG TLELGVDYGR ANLRDNYRLV DGASKDGWLF TAEHTQSVLK 
       260        270        280        290        300
GFNKFVVQYA TDSMTSQGKG LSQGSGVAFD NEKFAYNINN NGHMLRILDH 
       310        320        330        340        350
GAISMGDNWD MMYVGMYQDI NWDNDNGTKW WTVGIRPMYK WTPIMSTVME 
       360        370        380        390        400
IGYDNVESQR TGDKNNQYKI TLAQQWQAGD SIWSRPAIRV FATYAKWDEK 
       410        420        430        440 
WGYDYTGNAD NNANFGKAVP ADFNGGSFGR GDSDEWTFGA QMEIWW
Length:446
Mass (Da):49,912
Last modified:July 21, 1986 - 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:iB2D4E4F120DA494E
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 conflicti381S → T in AAC43130 (PubMed:8265357).Curated1

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
M16643 Genomic DNA Translation: AAA24059.1
M26131 Genomic DNA Translation: AAA24060.1
V00298 Genomic DNA Translation: CAA23575.1
J01648 Genomic DNA Translation: AAB59058.1
U00006 Genomic DNA Translation: AAC43130.1
U00096 Genomic DNA Translation: AAC77006.1
AP009048 Genomic DNA Translation: BAE78038.1
M24997 Genomic DNA Translation: AAC41396.1
V00297 Genomic DNA Translation: CAA23574.1

Protein sequence database of the Protein Information Resource

More...PIRi		A03443, QRECL

NCBI Reference Sequences

More...RefSeqi		NP_418460.1, NC_000913.3
WP_000973663.1, NZ_SSZK01000016.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC77006; AAC77006; b4036
BAE78038; BAE78038; BAE78038

Database of genes from NCBI RefSeq genomes

More...GeneIDi		948548

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3996
eco:b4036

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2674

<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
M16643 Genomic DNA Translation: AAA24059.1
M26131 Genomic DNA Translation: AAA24060.1
V00298 Genomic DNA Translation: CAA23575.1
J01648 Genomic DNA Translation: AAB59058.1
U00006 Genomic DNA Translation: AAC43130.1
U00096 Genomic DNA Translation: AAC77006.1
AP009048 Genomic DNA Translation: BAE78038.1
M24997 Genomic DNA Translation: AAC41396.1
V00297 Genomic DNA Translation: CAA23574.1
PIRiA03443, QRECL
RefSeqiNP_418460.1, NC_000913.3
WP_000973663.1, NZ_SSZK01000016.1

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
1AF6X-ray2.40A/B/C26-446[»]
1MALX-ray3.10A/B/C26-446[»]
1MPMX-ray2.60A/B/C26-446[»]
1MPNX-ray3.20A/B/C26-446[»]
1MPOX-ray2.80A/B/C26-446[»]
1MPQX-ray3.00A/B/C26-446[»]
SMRiP02943
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262663, 259 interactors
DIPiDIP-10082N
IntActiP02943, 3 interactors
STRINGi511145.b4036

Chemistry databases

DrugBankiDB02379, Beta-D-Glucose
DB04173, Fructose

Protein family/group databases

TCDBi1.B.3.1.1, the sugar porin (sp) family

Proteomic databases

jPOSTiP02943
PaxDbiP02943
PRIDEiP02943

Genome annotation databases

EnsemblBacteriaiAAC77006; AAC77006; b4036
BAE78038; BAE78038; BAE78038
GeneIDi948548
KEGGiecj:JW3996
eco:b4036
PATRICifig|1411691.4.peg.2674

Organism-specific databases

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

More...EchoBASEi		EB0523

Phylogenomic databases

eggNOGiCOG4580, Bacteria
HOGENOMiCLU_032473_4_1_6

Enzyme and pathway databases

BioCyciEcoCyc:EG10528-MONOMER
MetaCyc:EG10528-MONOMER

Miscellaneous databases

EvolutionaryTraceiP02943

Protein Ontology

More...PROi		PR:P02943

Family and domain databases

CDDicd01346, Maltoporin-like, 1 hit
Gene3Di2.40.170.10, 1 hit
HAMAPiMF_01301, LamB, 1 hit
InterProiView protein in InterPro
IPR023738, Maltoporin
IPR003192, Porin_LamB
IPR036998, Porin_LamB_sf
PfamiView protein in Pfam
PF02264, LamB, 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 nameiLAMB_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: P02943
Secondary accession number(s): Q2M6R8
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 2, 2021
This is version 200 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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