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Protein

Trehalose/maltose import ATP-binding protein MalK

Gene

malK

Organism
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the ABC transporter complex MalEFGK involved in trehalose/maltose import. Responsible for energy coupling to the transport system.3 Publications

Catalytic activityi

ATP + H2O + maltose(Out) = ADP + phosphate + maltose(In).

Enzyme regulationi

Inhibited by N-ethylmaleimide but not by vanadate.1 Publication

Kineticsi

  1. KM=155 µM for ATP1 Publication
  2. KM=430 µM for GTP1 Publication
  3. KM=870 µM for CTP1 Publication
  1. Vmax=0.55 µmol/min/mg enzyme with ATP as substrate1 Publication
  2. Vmax=0.45 µmol/min/mg enzyme with GTP as substrate1 Publication
  3. Vmax=0.32 µmol/min/mg enzyme with CTP as substrate1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

Temperature dependencei

Optimum temperature is 80 degrees Celsius.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 438ATPPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Sugar transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKQ9YGA6.

Names & Taxonomyi

Protein namesi
Recommended name:
Trehalose/maltose import ATP-binding protein MalK (EC:3.6.3.19)
Gene namesi
Name:malK
ORF Names:OCC_13985
OrganismiThermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
Taxonomic identifieri523849 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
Proteomesi
  • UP000015502 Componenti: Chromosome

Subcellular locationi

  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Trehalose/maltose import ATP-binding protein MalKPRO_0000421285Add
BLAST

Expressioni

Inductioni

Induced by maltose and trehalose.1 Publication

Interactioni

Subunit structurei

Homodimer. The complex is composed of two ATP-binding proteins (MalK), two transmembrane proteins (MalG and MalF) and a solute-binding protein (MalE).3 Publications

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1312Combined sources
Beta strandi16 – 2712Combined sources
Beta strandi31 – 355Combined sources
Helixi42 – 509Combined sources
Beta strandi56 – 627Combined sources
Beta strandi65 – 695Combined sources
Helixi70 – 723Combined sources
Helixi78 – 803Combined sources
Beta strandi81 – 866Combined sources
Helixi98 – 10811Combined sources
Helixi113 – 12614Combined sources
Helixi130 – 1323Combined sources
Helixi137 – 1393Combined sources
Helixi142 – 15514Combined sources
Beta strandi159 – 1646Combined sources
Turni166 – 1694Combined sources
Helixi172 – 18918Combined sources
Beta strandi192 – 1987Combined sources
Helixi200 – 2067Combined sources
Beta strandi208 – 2147Combined sources
Beta strandi217 – 2226Combined sources
Helixi224 – 2296Combined sources
Helixi234 – 2396Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi246 – 2527Combined sources
Beta strandi256 – 2594Combined sources
Beta strandi264 – 2663Combined sources
Helixi269 – 2779Combined sources
Beta strandi283 – 2897Combined sources
Helixi291 – 2933Combined sources
Beta strandi294 – 2963Combined sources
Turni297 – 2993Combined sources
Turni305 – 3073Combined sources
Beta strandi308 – 31912Combined sources
Beta strandi324 – 3307Combined sources
Beta strandi333 – 3397Combined sources
Beta strandi350 – 3556Combined sources
Helixi357 – 3593Combined sources
Beta strandi361 – 3644Combined sources
Turni365 – 3673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G29X-ray1.901/21-372[»]
ProteinModelPortaliQ9YGA6.
SMRiQ9YGA6. Positions 1-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9YGA6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 240237ABC transporterPROSITE-ProRule annotationAdd
BLAST

Domaini

Contains an N-terminal ATPase domain and a C-terminal regulatory domain.1 Publication

Sequence similaritiesi

Contains 1 ABC transporter domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK10112.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR008995. Mo/tungstate-bd_C_term_dom.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR013611. Transp-assoc_OB_typ2.
[Graphical view]
PfamiPF00005. ABC_tran. 1 hit.
PF08402. TOBE_2. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50331. SSF50331. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9YGA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVRLVDVW KVFGEVTAVR EMSLEVKDGE FMILLGPSGC GKTTTLRMIA
60 70 80 90 100
GLEEPSRGQI YIGDKLVADP EKGIFVPPKD RDIAMVFQSY ALYPHMTVYD
110 120 130 140 150
NIAFPLKLRK VPRQEIDQRV REVAELLGLT ELLNRKPREL SGGQRQRVAL
160 170 180 190 200
GRAIVRKPQV FLMDEPLSNL DAKLRVRMRA ELKKLQRQLG VTTIYVTHDQ
210 220 230 240 250
VEAMTMGDRI AVMNRGVLQQ VGSPDEVYDK PANTFVAGFI GSPPMNFLDA
260 270 280 290 300
IVTEDGFVDF GEFRLKLLPD QFEVLGELGY VGREVIFGIR PEDLYDAMFA
310 320 330 340 350
QVRVPGENLV RAVVEIVENL GSERIVHLRV GGVTFVGSFR SESRVREGVE
360 370
VDVVFDMKKI HIFDKTTGKA IF
Length:372
Mass (Da):41,786
Last modified:November 1, 1999 - v1
Checksum:i31261E66048BC76F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221M → L in AAD24578 (PubMed:10400644).Curated
Sequence conflicti22 – 221M → L in AAG45393 (PubMed:11115105).Curated
Sequence conflicti65 – 651K → R in AAD24578 (PubMed:10400644).Curated
Sequence conflicti65 – 651K → R in AAG45393 (PubMed:11115105).Curated
Sequence conflicti301 – 3011Q → R in AAD24578 (PubMed:10400644).Curated
Sequence conflicti301 – 3011Q → R in AAG45393 (PubMed:11115105).Curated
Sequence conflicti338 – 3381S → A in AAD24578 (PubMed:10400644).Curated
Sequence conflicti338 – 3381S → A in AAG45393 (PubMed:11115105).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121946 Genomic DNA. Translation: AAD23570.1.
AF126010 Genomic DNA. Translation: AAD24578.1.
AF307053 Genomic DNA. Translation: AAG45393.1.
AB054186 Genomic DNA. Translation: BAC10984.1.
CP006670 Genomic DNA. Translation: AGT34279.1.
RefSeqiWP_020953704.1. NC_022084.1.

Genome annotation databases

EnsemblBacteriaiAGT34279; AGT34279; OCC_13985.
GeneIDi16549639.
KEGGitlt:OCC_13985.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121946 Genomic DNA. Translation: AAD23570.1.
AF126010 Genomic DNA. Translation: AAD24578.1.
AF307053 Genomic DNA. Translation: AAG45393.1.
AB054186 Genomic DNA. Translation: BAC10984.1.
CP006670 Genomic DNA. Translation: AGT34279.1.
RefSeqiWP_020953704.1. NC_022084.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G29X-ray1.901/21-372[»]
ProteinModelPortaliQ9YGA6.
SMRiQ9YGA6. Positions 1-372.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAGT34279; AGT34279; OCC_13985.
GeneIDi16549639.
KEGGitlt:OCC_13985.

Phylogenomic databases

KOiK10112.

Enzyme and pathway databases

SABIO-RKQ9YGA6.

Miscellaneous databases

EvolutionaryTraceiQ9YGA6.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR008995. Mo/tungstate-bd_C_term_dom.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR013611. Transp-assoc_OB_typ2.
[Graphical view]
PfamiPF00005. ABC_tran. 1 hit.
PF08402. TOBE_2. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50331. SSF50331. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular and biochemical analysis of MalK, the ATP-hydrolyzing subunit of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis."
    Greller G., Horlacher R., DiRuggiero J., Boos W.
    J. Biol. Chem. 274:20259-20264(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ATPASE ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
    Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
  3. "Molecular evolution of the ATPase subunit of three archaeal sugar ABC transporters."
    Imamura H., Jeon B.S., Wakagi T.
    Biochem. Biophys. Res. Commun. 319:230-234(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
  4. "Genome sequence of the model hyperthermophilic archaeon Thermococcus litoralis NS-C."
    Gardner A.F., Kumar S., Perler F.B.
    J. Bacteriol. 194:2375-2376(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
  5. "High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis."
    Xavier K.B., Martins L.O., Peist R., Kossmann M., Boos W., Santos H.
    J. Bacteriol. 178:4773-4777(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
  6. "Purification and characterization of the heterologously expressed trehalose/maltose ABC transporter complex of the hyperthermophilic archaeon Thermococcus litoralis."
    Greller G., Riek R., Boos W.
    Eur. J. Biochem. 268:4011-4018(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  7. "Crystallization and preliminary X-ray analysis of the trehalose/maltose ABC transporter MalFGK2 from Thermococcus litoralis."
    Schiefner A., Diederichs K., Hashimoto K., Boos W., Welte W.
    Acta Crystallogr. D 58:2147-2149(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, SUBUNIT.
  8. "Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis."
    Diederichs K., Diez J., Greller G., Muller C., Breed J., Schnell C., Vonrhein C., Boos W., Welte W.
    EMBO J. 19:5951-5961(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), SUBUNIT, DOMAIN.

Entry informationi

Entry nameiMALK_THELN
AccessioniPrimary (citable) accession number: Q9YGA6
Secondary accession number(s): Q9V306, S5ZTR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

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.