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Protein
Submitted name:

Maltose binding protein

Gene

malE

Organism
Alicyclobacillus acidocaldarius (Bacillus acidocaldarius)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Maltose binding proteinImported
Gene namesi
Name:malEImported
OrganismiAlicyclobacillus acidocaldarius (Bacillus acidocaldarius)Imported
Taxonomic identifieri1388 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesAlicyclobacillaceaeAlicyclobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 427403Sequence analysisPRO_5004331483Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi1048834.TC41_3216.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1URDX-ray1.53A/B55-424[»]
1URGX-ray1.80A26-427[»]
1URSX-ray1.45A/B26-427[»]
ProteinModelPortaliQ9RHZ6.
SMRiQ9RHZ6. Positions 55-427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RHZ6.

Family & Domainsi

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiENOG4107FKK. Bacteria.
COG2182. LUCA.

Family and domain databases

InterProiIPR006060. Maltose-bd.
IPR006059. SBP_1_dom.
[Graphical view]
PfamiPF01547. SBP_bac_1. 1 hit.
[Graphical view]
PRINTSiPR00181. MALTOSEBP.

Sequencei

Sequence statusi: Complete.

Q9RHZ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVRRWGIVS TGVAALVLAG GAIAGCGTSN GGQNTSPSTS SSSAKGEASA
60 70 80 90 100
LPKGQTITVW SWQTGPELQD VKQIAAQWAK AHGDKVIVVD QSSNPKGFQF
110 120 130 140 150
YATAARTGKG PDVVFGMPHD NNGVFAEEGL MAPVPSGVLN TGLYAPNTID
160 170 180 190 200
AIKVNGTMYS VPVSVQVAAI YYNKKLVPQP PQTWAEFVKD ANAHGFMYDQ
210 220 230 240 250
ANLYFDYAII GGYGGYVFKD NNGTLDPNNI GLDTPGAVQA YTLMRDMVSK
260 270 280 290 300
YHWMTPSTNG SIAKAEFLAG KIGMYVSGPW DTADIEKAKI DFGVTPWPTL
310 320 330 340 350
PNGKHATPFL GVITAFVNKE SKTQAADWSL VQALTSAQAQ QMYFRDSQQI
360 370 380 390 400
PALLSVQRSS AVQSSPTFKA FVEQLRYAVP MPNIPQMQAV WQAMSILQNI
410 420
IAGKVSPEQG AKDFVQNIQK GIMAQGS
Length:427
Mass (Da):45,674
Last modified:May 1, 2000 - v1
Checksum:iF0CCD5BA88BF952C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ252161 Genomic DNA. Translation: CAB65651.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ252161 Genomic DNA. Translation: CAB65651.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1URDX-ray1.53A/B55-424[»]
1URGX-ray1.80A26-427[»]
1URSX-ray1.45A/B26-427[»]
ProteinModelPortaliQ9RHZ6.
SMRiQ9RHZ6. Positions 55-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1048834.TC41_3216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107FKK. Bacteria.
COG2182. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ9RHZ6.

Family and domain databases

InterProiIPR006060. Maltose-bd.
IPR006059. SBP_1_dom.
[Graphical view]
PfamiPF01547. SBP_bac_1. 1 hit.
[Graphical view]
PRINTSiPR00181. MALTOSEBP.
ProtoNetiSearch...

Publicationsi

  1. "Maltose and maltodextrin transport in the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius is mediated by a high-affinity transport system that includes a maltose binding protein tolerant to low pH."
    Huelsmann A., Lurz R., Scheffel F., Schneider E.
    J. Bacteriol. 182:6292-6301(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 27009Imported.
  2. "X-ray structures of the maltose-maltodextrin-binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius provide insight into acid stability of proteins."
    Schafer K., Magnusson U., Scheffel F., Schiefner A., Sandgren M.O., Diederichs K., Welte W., Hulsmann A., Schneider E., Mowbray S.L.
    J. Mol. Biol. 335:261-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 26-427.

Entry informationi

Entry nameiQ9RHZ6_ALIAC
AccessioniPrimary (citable) accession number: Q9RHZ6
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: March 16, 2016
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.