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Protein

D-galactose-binding periplasmic protein

Gene

mglB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This protein is involved in the active transport of galactose and glucose. It plays a role in the chemotaxis towards the two sugars by interacting with the trg chemoreceptor.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei97 – 971Interacts with membrane-bound trg signal transducer

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi157 – 1659First part of site
Calcium bindingi227 – 2282Second part of site

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Sugar transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2203-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
D-galactose-binding periplasmic protein
Short name:
GBP
Alternative name(s):
D-galactose/ D-glucose-binding protein
Short name:
GGBP
Gene namesi
Name:mglB
Ordered Locus Names:STM2190
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 332309D-galactose-binding periplasmic proteinPRO_0000031723Add
BLAST

Proteomic databases

PaxDbiP23905.
PRIDEiP23905.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM2190.

Structurei

Secondary structure

1
332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 338Combined sources
Helixi38 – 5215Combined sources
Beta strandi57 – 637Combined sources
Helixi68 – 8013Combined sources
Beta strandi84 – 885Combined sources
Helixi93 – 953Combined sources
Helixi96 – 10510Combined sources
Beta strandi110 – 1156Combined sources
Helixi119 – 1235Combined sources
Beta strandi128 – 1325Combined sources
Helixi135 – 15218Combined sources
Helixi154 – 1563Combined sources
Beta strandi161 – 17010Combined sources
Helixi176 – 19116Combined sources
Beta strandi196 – 2038Combined sources
Helixi208 – 21912Combined sources
Helixi224 – 2263Combined sources
Beta strandi229 – 2346Combined sources
Helixi235 – 24713Combined sources
Helixi262 – 2698Combined sources
Beta strandi275 – 2784Combined sources
Helixi281 – 29616Combined sources
Turni301 – 3044Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi319 – 3213Combined sources
Turni323 – 3253Combined sources
Helixi326 – 3283Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GCAX-ray1.70A24-332[»]
1GCGX-ray1.90A24-332[»]
3GA5X-ray1.87A/B24-332[»]
3GBPX-ray2.40A24-330[»]
ProteinModelPortaliP23905.
SMRiP23905. Positions 24-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23905.

Family & Domainsi

Domaini

The calcium-binding site is structurally similar to that of EF-hand proteins, but is in two parts, with the last calcium ligand provided by Glu-228.

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105EMA. Bacteria.
COG1879. LUCA.
HOGENOMiHOG000212345.
KOiK10540.
OMAiAMWDTAM.
OrthoDBiEOG6G7R0P.
PhylomeDBiP23905.

Family and domain databases

InterProiIPR028082. Peripla_BP_I.
IPR025997. SBP_2_dom.
[Graphical view]
PfamiPF13407. Peripla_BP_4. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23905-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKKVLTLSA VMASLLFGAH AHAADTRIGV TIYKYDDNFM SVVRKAIEKD
60 70 80 90 100
GKSAPDVQLL MNDSQNDQSK QNDQIDVLLA KGVKALAINL VDPAAAGTVI
110 120 130 140 150
EKARGQNVPV VFFNKEPSRK ALDSYDKAYY VGTDSKESGV IQGDLIAKHW
160 170 180 190 200
QANQGWDLNK DGKIQYVLLK GEPGHPDAEA RTTYVVKELN DKGIQTEQLA
210 220 230 240 250
LDTAMWDTAQ AKDKMDAWLS GPNANKIEVV IANNDAMAMG AVEALKAHNK
260 270 280 290 300
SSIPVFGVDA LPEALALVKS GAMAGTVLND ANNQAKATFD LAKNLAEGKG
310 320 330
AADGTSWKIE NKIVRVPYVG VDKDNLSEFT QK
Length:332
Mass (Da):35,814
Last modified:January 23, 2002 - v2
Checksum:iCF31E994E00992D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1751H → A (PubMed:3146019).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL21094.1.
PIRiS29390.
RefSeqiNP_461135.1. NC_003197.1.
WP_001036943.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21094; AAL21094; STM2190.
GeneIDi1253712.
KEGGistm:STM2190.
PATRICi32382973. VBISalEnt20916_2317.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL21094.1.
PIRiS29390.
RefSeqiNP_461135.1. NC_003197.1.
WP_001036943.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GCAX-ray1.70A24-332[»]
1GCGX-ray1.90A24-332[»]
3GA5X-ray1.87A/B24-332[»]
3GBPX-ray2.40A24-330[»]
ProteinModelPortaliP23905.
SMRiP23905. Positions 24-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM2190.

Proteomic databases

PaxDbiP23905.
PRIDEiP23905.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL21094; AAL21094; STM2190.
GeneIDi1253712.
KEGGistm:STM2190.
PATRICi32382973. VBISalEnt20916_2317.

Phylogenomic databases

eggNOGiENOG4105EMA. Bacteria.
COG1879. LUCA.
HOGENOMiHOG000212345.
KOiK10540.
OMAiAMWDTAM.
OrthoDBiEOG6G7R0P.
PhylomeDBiP23905.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2203-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP23905.

Family and domain databases

InterProiIPR028082. Peripla_BP_I.
IPR025997. SBP_2_dom.
[Graphical view]
PfamiPF13407. Peripla_BP_4. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mglB sequence of Salmonella typhimurium LT2; promoter analysis by gene fusions and evidence for a divergently oriented gene coding for the mgl repressor."
    Benner-Luger D., Boos W.
    Mol. Gen. Genet. 214:579-587(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "The X-ray structure of the periplasmic galactose binding protein from Salmonella typhimurium at 3.0-A resolution."
    Mowbray S.L., Petsko G.A.
    J. Biol. Chem. 258:7991-7997(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  4. "The 1.7 A refined X-ray structure of the periplasmic glucose/galactose receptor from Salmonella typhimurium."
    Zhou J.Y., Flocco M.M., Mowbray S.L.
    J. Mol. Biol. 233:739-752(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  5. "The 1.9 A X-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium."
    Flocco M.M., Mowbray S.L.
    J. Biol. Chem. 269:8931-8936(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiDGAL_SALTY
AccessioniPrimary (citable) accession number: P23905
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2002
Last modified: December 9, 2015
This is version 116 of the entry and version 2 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.