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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 43ATPPROSITE-ProRule annotation8

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004212851 – 372Trehalose/maltose import ATP-binding protein MalKAdd BLAST372

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

1372
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 13Combined sources12
Beta strandi16 – 27Combined sources12
Beta strandi31 – 35Combined sources5
Helixi42 – 50Combined sources9
Beta strandi56 – 62Combined sources7
Beta strandi65 – 69Combined sources5
Helixi70 – 72Combined sources3
Helixi78 – 80Combined sources3
Beta strandi81 – 86Combined sources6
Helixi98 – 108Combined sources11
Helixi113 – 126Combined sources14
Helixi130 – 132Combined sources3
Helixi137 – 139Combined sources3
Helixi142 – 155Combined sources14
Beta strandi159 – 164Combined sources6
Turni166 – 169Combined sources4
Helixi172 – 189Combined sources18
Beta strandi192 – 198Combined sources7
Helixi200 – 206Combined sources7
Beta strandi208 – 214Combined sources7
Beta strandi217 – 222Combined sources6
Helixi224 – 229Combined sources6
Helixi234 – 239Combined sources6
Beta strandi240 – 243Combined sources4
Beta strandi246 – 252Combined sources7
Beta strandi256 – 259Combined sources4
Beta strandi264 – 266Combined sources3
Helixi269 – 277Combined sources9
Beta strandi283 – 289Combined sources7
Helixi291 – 293Combined sources3
Beta strandi294 – 296Combined sources3
Turni297 – 299Combined sources3
Turni305 – 307Combined sources3
Beta strandi308 – 319Combined sources12
Beta strandi324 – 330Combined sources7
Beta strandi333 – 339Combined sources7
Beta strandi350 – 355Combined sources6
Helixi357 – 359Combined sources3
Beta strandi361 – 364Combined sources4
Turni365 – 367Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9YGA6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 240ABC transporterPROSITE-ProRule annotationAdd BLAST237

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

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR008995. Mo/tungstate-bd_C_term_dom.
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)DescriptionActionsGraphical viewLength
Sequence conflicti22M → L in AAD24578 (PubMed:10400644).Curated1
Sequence conflicti22M → L in AAG45393 (PubMed:11115105).Curated1
Sequence conflicti65K → R in AAD24578 (PubMed:10400644).Curated1
Sequence conflicti65K → R in AAG45393 (PubMed:11115105).Curated1
Sequence conflicti301Q → R in AAD24578 (PubMed:10400644).Curated1
Sequence conflicti301Q → R in AAG45393 (PubMed:11115105).Curated1
Sequence conflicti338S → A in AAD24578 (PubMed:10400644).Curated1
Sequence conflicti338S → A in AAG45393 (PubMed:11115105).Curated1

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.

Genome annotation databases

EnsemblBacteriaiAGT34279; AGT34279; OCC_13985.
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.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAGT34279; AGT34279; OCC_13985.
KEGGitlt:OCC_13985.

Phylogenomic databases

KOiK10112.

Enzyme and pathway databases

SABIO-RKQ9YGA6.

Miscellaneous databases

EvolutionaryTraceiQ9YGA6.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR008995. Mo/tungstate-bd_C_term_dom.
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...

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: November 2, 2016
This is version 110 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.