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Protein

Maltose transport system permease protein MalF

Gene

malF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane.

GO - Molecular functioni

  • maltose-transporting ATPase activity Source: EcoCyc

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • maltodextrin transport Source: EcoCyc
  • maltose transport Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:MALF-MONOMER.
ECOL316407:JW3993-MONOMER.
MetaCyc:MALF-MONOMER.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Maltose transport system permease protein MalF
Gene namesi
Name:malF
Ordered Locus Names:b4033, JW3993
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10555. malF.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicCuratedAdd
BLAST
Transmembranei17 – 3620HelicalCuratedAdd
BLAST
Topological domaini37 – 393PeriplasmicCurated
Transmembranei40 – 5819HelicalCuratedAdd
BLAST
Topological domaini59 – 668CytoplasmicCurated
Transmembranei67 – 9226HelicalCuratedAdd
BLAST
Topological domaini93 – 275183PeriplasmicCuratedAdd
BLAST
Transmembranei276 – 30631HelicalCuratedAdd
BLAST
Topological domaini307 – 31812CytoplasmicCuratedAdd
BLAST
Transmembranei319 – 33618HelicalCuratedAdd
BLAST
Topological domaini337 – 36933PeriplasmicCuratedAdd
BLAST
Transmembranei370 – 39223HelicalCuratedAdd
BLAST
Topological domaini393 – 42533CytoplasmicCuratedAdd
BLAST
Transmembranei426 – 45227HelicalCuratedAdd
BLAST
Topological domaini453 – 48331PeriplasmicCuratedAdd
BLAST
Transmembranei484 – 50522HelicalCuratedAdd
BLAST
Topological domaini506 – 5149CytoplasmicCurated

GO - Cellular componenti

  • ATP-binding cassette (ABC) transporter complex Source: EcoCyc
  • ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing Source: GO_Central
  • integral component of plasma membrane Source: EcoCyc
  • maltose transport complex Source: EcoCyc
  • membrane Source: UniProtKB
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi334 – 3341L → W: Ability to transport lactose in a saturable manner. 1 Publication
Mutagenesisi372 – 3721L → W: Growth on maltose but not on media containing either maltoheptaose or maltoheptaose plus maltose. 1 Publication
Mutagenesisi376 – 3761N → K or H: No growth on maltose. 1 Publication
Mutagenesisi380 – 3801G → C or S: No growth on maltose. 1 Publication
Mutagenesisi401 – 4011E → A, C, K or L: Reduction of transport rate. 2 Publications
Mutagenesisi403 – 4031S → C, D, K or L: Reduction of transport rate. 2 Publications
Mutagenesisi407 – 4071G → A or P: No effect. 1 Publication
Mutagenesisi420 – 4201P → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 514514Maltose transport system permease protein MalFPRO_0000060068Add
BLAST

Proteomic databases

PaxDbiP02916.

Interactioni

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
malEP0AEX92EBI-1118919,EBI-369910

Protein-protein interaction databases

BioGridi4261701. 10 interactions.
DIPiDIP-10142N.
IntActiP02916. 5 interactions.
STRINGi511145.b4033.

Structurei

Secondary structure

1
514
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2916Combined sources
Helixi31 – 355Combined sources
Turni36 – 383Combined sources
Helixi40 – 5819Combined sources
Helixi60 – 623Combined sources
Helixi65 – 7814Combined sources
Helixi80 – 8910Combined sources
Beta strandi95 – 984Combined sources
Helixi102 – 11110Combined sources
Beta strandi113 – 12715Combined sources
Beta strandi130 – 1378Combined sources
Turni138 – 1414Combined sources
Beta strandi142 – 1465Combined sources
Beta strandi153 – 16412Combined sources
Helixi173 – 1786Combined sources
Helixi180 – 1834Combined sources
Beta strandi186 – 1894Combined sources
Beta strandi191 – 1933Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi200 – 21314Combined sources
Beta strandi215 – 2173Combined sources
Beta strandi219 – 2213Combined sources
Turni222 – 2243Combined sources
Beta strandi227 – 2315Combined sources
Turni232 – 2354Combined sources
Beta strandi236 – 2394Combined sources
Beta strandi250 – 2534Combined sources
Helixi262 – 2698Combined sources
Turni272 – 2765Combined sources
Helixi277 – 30630Combined sources
Beta strandi309 – 3113Combined sources
Helixi314 – 3229Combined sources
Helixi323 – 3253Combined sources
Helixi329 – 33911Combined sources
Beta strandi342 – 3454Combined sources
Helixi346 – 3538Combined sources
Beta strandi354 – 3563Combined sources
Turni361 – 3633Combined sources
Helixi365 – 39127Combined sources
Helixi392 – 3943Combined sources
Helixi397 – 4059Combined sources
Helixi410 – 4167Combined sources
Helixi418 – 43821Combined sources
Helixi441 – 4477Combined sources
Turni448 – 4503Combined sources
Beta strandi452 – 4543Combined sources
Beta strandi462 – 4643Combined sources
Helixi467 – 4759Combined sources
Beta strandi477 – 4804Combined sources
Helixi484 – 50118Combined sources
Turni502 – 5043Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R6GX-ray2.80F1-514[»]
3FH6X-ray4.50F/H36-514[»]
3PUVX-ray2.40F1-514[»]
3PUWX-ray2.30F1-514[»]
3PUXX-ray2.30F1-514[»]
3PUYX-ray3.10F1-514[»]
3PUZX-ray2.90F1-514[»]
3PV0X-ray3.10F1-514[»]
3RLFX-ray2.20F1-514[»]
4JBWX-ray3.91F/H1-514[»]
4KHZX-ray2.90F1-514[»]
4KI0X-ray2.38F1-514[»]
ProteinModelPortaliP02916.
SMRiP02916. Positions 13-514.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02916.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini281 – 505225ABC transmembrane type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ABC transmembrane type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D56. Bacteria.
COG1175. LUCA.
HOGENOMiHOG000239267.
InParanoidiP02916.
KOiK10109.
OMAiTMILIVN.
OrthoDBiEOG6VMTK6.
PhylomeDBiP02916.

Family and domain databases

Gene3Di1.10.3720.10. 1 hit.
InterProiIPR029345. MalF_P2.
IPR000515. MetI-like.
[Graphical view]
PfamiPF00528. BPD_transp_1. 1 hit.
PF14785. MalF_P2. 1 hit.
[Graphical view]
SUPFAMiSSF161098. SSF161098. 1 hit.
PROSITEiPS50928. ABC_TM1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02916-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVIKKKHWW QSDALKWSVL GLLGLLVGYL VVLMYAQGEY LFAITTLILS
60 70 80 90 100
SAGLYIFANR KAYAWRYVYP GMAGMGLFVL FPLVCTIAIA FTNYSSTNQL
110 120 130 140 150
TFERAQEVLL DRSWQAGKTY NFGLYPAGDE WQLALSDGET GKNYLSDAFK
160 170 180 190 200
FGGEQKLQLK ETTAQPEGER ANLRVITQNR QALSDITAIL PDGNKVMMSS
210 220 230 240 250
LRQFSGTQPL YTLDGDGTLT NNQSGVKYRP NNQIGFYQSI TADGNWGDEK
260 270 280 290 300
LSPGYTVTTG WKNFTRVFTD EGIQKPFLAI FVWTVVFSLI TVFLTVAVGM
310 320 330 340 350
VLACLVQWEA LRGKAVYRVL LILPYAVPSF ISILIFKGLF NQSFGEINMM
360 370 380 390 400
LSALFGVKPA WFSDPTTART MLIIVNTWLG YPYMMILCMG LLKAIPDDLY
410 420 430 440 450
EASAMDGAGP FQNFFKITLP LLIKPLTPLM IASFAFNFNN FVLIQLLTNG
460 470 480 490 500
GPDRLGTTTP AGYTDLLVNY TYRIAFEGGG GQDFGLAAAI ATLIFLLVGA
510
LAIVNLKATR MKFD
Length:514
Mass (Da):57,013
Last modified:July 21, 1986 - v1
Checksum:i895CEA1986CE5C0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01648 Genomic DNA. Translation: AAB59055.1.
U00006 Genomic DNA. Translation: AAC43127.1.
U00096 Genomic DNA. Translation: AAC77003.1.
AP009048 Genomic DNA. Translation: BAE78035.1.
X02871 Genomic DNA. Translation: CAA26627.1.
PIRiA03414. MMECMF.
RefSeqiNP_418457.1. NC_000913.3.
WP_001297290.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77003; AAC77003; b4033.
BAE78035; BAE78035; BAE78035.
GeneIDi948532.
KEGGiecj:JW3993.
eco:b4033.
PATRICi32123599. VBIEscCol129921_4148.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01648 Genomic DNA. Translation: AAB59055.1.
U00006 Genomic DNA. Translation: AAC43127.1.
U00096 Genomic DNA. Translation: AAC77003.1.
AP009048 Genomic DNA. Translation: BAE78035.1.
X02871 Genomic DNA. Translation: CAA26627.1.
PIRiA03414. MMECMF.
RefSeqiNP_418457.1. NC_000913.3.
WP_001297290.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R6GX-ray2.80F1-514[»]
3FH6X-ray4.50F/H36-514[»]
3PUVX-ray2.40F1-514[»]
3PUWX-ray2.30F1-514[»]
3PUXX-ray2.30F1-514[»]
3PUYX-ray3.10F1-514[»]
3PUZX-ray2.90F1-514[»]
3PV0X-ray3.10F1-514[»]
3RLFX-ray2.20F1-514[»]
4JBWX-ray3.91F/H1-514[»]
4KHZX-ray2.90F1-514[»]
4KI0X-ray2.38F1-514[»]
ProteinModelPortaliP02916.
SMRiP02916. Positions 13-514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261701. 10 interactions.
DIPiDIP-10142N.
IntActiP02916. 5 interactions.
STRINGi511145.b4033.

Protein family/group databases

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

Proteomic databases

PaxDbiP02916.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77003; AAC77003; b4033.
BAE78035; BAE78035; BAE78035.
GeneIDi948532.
KEGGiecj:JW3993.
eco:b4033.
PATRICi32123599. VBIEscCol129921_4148.

Organism-specific databases

EchoBASEiEB0550.
EcoGeneiEG10555. malF.

Phylogenomic databases

eggNOGiENOG4105D56. Bacteria.
COG1175. LUCA.
HOGENOMiHOG000239267.
InParanoidiP02916.
KOiK10109.
OMAiTMILIVN.
OrthoDBiEOG6VMTK6.
PhylomeDBiP02916.

Enzyme and pathway databases

BioCyciEcoCyc:MALF-MONOMER.
ECOL316407:JW3993-MONOMER.
MetaCyc:MALF-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02916.
PROiP02916.

Family and domain databases

Gene3Di1.10.3720.10. 1 hit.
InterProiIPR029345. MalF_P2.
IPR000515. MetI-like.
[Graphical view]
PfamiPF00528. BPD_transp_1. 1 hit.
PF14785. MalF_P2. 1 hit.
[Graphical view]
SUPFAMiSSF161098. SSF161098. 1 hit.
PROSITEiPS50928. ABC_TM1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of the gene for malF protein, an inner membrane component of the maltose transport system of Escherichia coli. Repeated DNA sequences are found in the malE-malF intercistronic region."
    Froshauer S., Beckwith J.
    J. Biol. Chem. 259:10896-10903(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems."
    Dassa E., Hofnung M.
    EMBO J. 4:2287-2293(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 469-514.
  6. "The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology."
    von Heijne G.
    EMBO J. 5:3021-3027(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  7. "Genetic analysis of membrane protein topology by a sandwich gene fusion approach."
    Ehrmann M., Boyd D., Beckwith J.
    Proc. Natl. Acad. Sci. U.S.A. 87:7574-7578(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  8. "Decoding signals for membrane protein assembly using alkaline phosphatase fusions."
    McGovern K., Ehrmann M., Beckwith J.
    EMBO J. 10:2773-2782(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  9. "Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits."
    Mourez M., Hofnung M., Dassa E.
    EMBO J. 16:3066-3077(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-401; SER-403; GLY-407 AND PRO-420.
  10. "Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system."
    Merino G., Shuman H.A.
    J. Bacteriol. 179:7687-7694(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-334.
  11. "Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis."
    Ehrle R., Pick C., Ulrich R., Hofmann E., Ehrmann M.
    J. Bacteriol. 178:2255-2262(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-372; ASN-376 AND GLY-380.
  12. "ATP modulates subunit-subunit interactions in an ATP-binding cassette transporter (MalFGK2) determined by site-directed chemical cross-linking."
    Hunke S., Mourez M., Jehanno M., Dassa E., Schneider E.
    J. Biol. Chem. 275:15526-15534(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT INTERACTION, MUTAGENESIS OF GLU-401 AND SER-403.
  13. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  14. "Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC."
    Wagner S., Pop O.I., Haan G.J., Baars L., Koningstein G., Klepsch M.M., Genevaux P., Luirink J., de Gier J.W.
    J. Biol. Chem. 283:17881-17890(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, REQUIREMENT FOR YIDC FOR PROTEIN AND COMPLEX FORMATION.
  15. "Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation."
    Boos W., Shuman H.
    Microbiol. Mol. Biol. Rev. 62:204-229(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiMALF_ECOLI
AccessioniPrimary (citable) accession number: P02916
Secondary accession number(s): Q2M6S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 16, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

When MalF EAA loop mutations are made concomitantly with MalG EAA loop mutations, a complete loss of transport and complex formation is observed, except for the Gly-407. This suggests that the MalF-MalG interaction may be important for the proper assembly and also for the correct function of the transporter.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.