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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10555. malF.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 16CytoplasmicCuratedAdd BLAST16
Transmembranei17 – 36HelicalCuratedAdd BLAST20
Topological domaini37 – 39PeriplasmicCurated3
Transmembranei40 – 58HelicalCuratedAdd BLAST19
Topological domaini59 – 66CytoplasmicCurated8
Transmembranei67 – 92HelicalCuratedAdd BLAST26
Topological domaini93 – 275PeriplasmicCuratedAdd BLAST183
Transmembranei276 – 306HelicalCuratedAdd BLAST31
Topological domaini307 – 318CytoplasmicCuratedAdd BLAST12
Transmembranei319 – 336HelicalCuratedAdd BLAST18
Topological domaini337 – 369PeriplasmicCuratedAdd BLAST33
Transmembranei370 – 392HelicalCuratedAdd BLAST23
Topological domaini393 – 425CytoplasmicCuratedAdd BLAST33
Transmembranei426 – 452HelicalCuratedAdd BLAST27
Topological domaini453 – 483PeriplasmicCuratedAdd BLAST31
Transmembranei484 – 505HelicalCuratedAdd BLAST22
Topological domaini506 – 514CytoplasmicCurated9

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)DescriptionActionsGraphical viewLength
Mutagenesisi334L → W: Ability to transport lactose in a saturable manner. 1 Publication1
Mutagenesisi372L → W: Growth on maltose but not on media containing either maltoheptaose or maltoheptaose plus maltose. 1 Publication1
Mutagenesisi376N → K or H: No growth on maltose. 1 Publication1
Mutagenesisi380G → C or S: No growth on maltose. 1 Publication1
Mutagenesisi401E → A, C, K or L: Reduction of transport rate. 2 Publications1
Mutagenesisi403S → C, D, K or L: Reduction of transport rate. 2 Publications1
Mutagenesisi407G → A or P: No effect. 1 Publication1
Mutagenesisi420P → A: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000600681 – 514Maltose transport system permease protein MalFAdd BLAST514

Proteomic databases

PaxDbiP02916.
PRIDEiP02916.

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 interactors.
DIPiDIP-10142N.
IntActiP02916. 5 interactors.
STRINGi511145.b4033.

Structurei

Secondary structure

1514
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 29Combined sources16
Helixi31 – 35Combined sources5
Turni36 – 38Combined sources3
Helixi40 – 58Combined sources19
Helixi60 – 62Combined sources3
Helixi65 – 78Combined sources14
Helixi80 – 89Combined sources10
Beta strandi95 – 98Combined sources4
Helixi102 – 111Combined sources10
Beta strandi113 – 127Combined sources15
Beta strandi130 – 137Combined sources8
Turni138 – 141Combined sources4
Beta strandi142 – 146Combined sources5
Beta strandi153 – 164Combined sources12
Helixi173 – 178Combined sources6
Helixi180 – 183Combined sources4
Beta strandi186 – 189Combined sources4
Beta strandi191 – 193Combined sources3
Beta strandi195 – 198Combined sources4
Beta strandi200 – 213Combined sources14
Beta strandi215 – 217Combined sources3
Beta strandi219 – 221Combined sources3
Turni222 – 224Combined sources3
Beta strandi227 – 231Combined sources5
Turni232 – 235Combined sources4
Beta strandi236 – 239Combined sources4
Beta strandi250 – 253Combined sources4
Helixi262 – 269Combined sources8
Turni272 – 276Combined sources5
Helixi277 – 306Combined sources30
Beta strandi309 – 311Combined sources3
Helixi314 – 322Combined sources9
Helixi323 – 325Combined sources3
Helixi329 – 339Combined sources11
Beta strandi342 – 345Combined sources4
Helixi346 – 353Combined sources8
Beta strandi354 – 356Combined sources3
Turni361 – 363Combined sources3
Helixi365 – 391Combined sources27
Helixi392 – 394Combined sources3
Helixi397 – 405Combined sources9
Helixi410 – 416Combined sources7
Helixi418 – 438Combined sources21
Helixi441 – 447Combined sources7
Turni448 – 450Combined sources3
Beta strandi452 – 454Combined sources3
Beta strandi462 – 464Combined sources3
Helixi467 – 475Combined sources9
Beta strandi477 – 480Combined sources4
Helixi484 – 501Combined sources18
Turni502 – 504Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02916.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini281 – 505ABC transmembrane type-1PROSITE-ProRule annotationAdd BLAST225

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.
PhylomeDBiP02916.

Family and domain databases

CDDicd06261. TM_PBP2. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

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

Proteomic databases

PaxDbiP02916.
PRIDEiP02916.

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.
PhylomeDBiP02916.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP02916.
PROiP02916.

Family and domain databases

CDDicd06261. TM_PBP2. 1 hit.
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...

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: November 2, 2016
This is version 149 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.