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Protein

Ectoine-binding periplasmic protein TeaA

Gene

teaA

Organism
Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of the tripartite ATP-independent periplasmic (TRAP) transport system TeaABC involved in the uptake of ectoine and hydroxyectoine in response to osmotic upshock. Probably functions as a recovery system for synthesized ectoine that leaks out of the cell. Binds ectoine with high affinity. Affinity for hydroxyectoine is approximately 20-fold lower.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341Ectoine
Binding sitei169 – 1691Ectoine
Binding sitei209 – 2091Ectoine
Binding sitei213 – 2131Ectoine
Binding sitei234 – 2341Ectoine

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

BioCyciHELO768066:GJEE-3356-MONOMER.

Protein family/group databases

TCDBi2.A.56.2.1. the tripartite atp-independent periplasmic transporter (trap-t) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Ectoine-binding periplasmic protein TeaA
Gene namesi
Name:teaA
Ordered Locus Names:HELO_4274
OrganismiHalomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)
Taxonomic identifieri768066 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHalomonadaceaeHalomonas
Proteomesi
  • UP000008707 Componenti: Chromosome

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

Deletion abolishes accumulation of ectoine from the medium.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi273 – 2753GLS → AAA: Strongly biased toward the open conformation. Has lower affinity for ectoine. Does not affect the structure of the substrate-binding site. 1 Publication
Mutagenesisi273 – 2731G → P: Conformationally unbiased. Has wild-type affinity for ectoine. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 341316Ectoine-binding periplasmic protein TeaAPRO_0000428828Add
BLAST

Interactioni

Subunit structurei

Monomer. The complex comprises the extracytoplasmic solute receptor protein TeaA, and the two transmembrane proteins TeaB and TeaC.2 Publications

Protein-protein interaction databases

STRINGi768066.HELO_4274.

Structurei

Secondary structure

1
341
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 315Combined sources
Helixi39 – 5315Combined sources
Beta strandi54 – 563Combined sources
Beta strandi58 – 625Combined sources
Turni64 – 674Combined sources
Helixi73 – 786Combined sources
Beta strandi83 – 875Combined sources
Helixi89 – 924Combined sources
Turni93 – 953Combined sources
Helixi97 – 1037Combined sources
Helixi112 – 12110Combined sources
Helixi123 – 1264Combined sources
Helixi128 – 1347Combined sources
Turni135 – 1373Combined sources
Beta strandi138 – 15518Combined sources
Helixi160 – 1634Combined sources
Beta strandi167 – 1704Combined sources
Helixi174 – 18310Combined sources
Beta strandi186 – 1894Combined sources
Helixi192 – 1943Combined sources
Helixi195 – 2006Combined sources
Beta strandi205 – 2106Combined sources
Helixi211 – 2166Combined sources
Helixi219 – 2213Combined sources
Beta strandi225 – 2284Combined sources
Beta strandi233 – 2419Combined sources
Helixi242 – 2476Combined sources
Helixi250 – 27122Combined sources
Helixi274 – 28512Combined sources
Beta strandi290 – 2934Combined sources
Helixi296 – 3038Combined sources
Helixi306 – 33429Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VPNX-ray1.55A/B26-341[»]
2VPOX-ray1.80A/B26-341[»]
3GYYX-ray2.20A/B/C/D1-341[»]
ProteinModelPortaliE1VBK1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108KJ1. Bacteria.
COG1638. LUCA.
HOGENOMiHOG000224244.
OMAiHEYQIRI.
OrthoDBiPOG091H03NF.

Family and domain databases

InterProiIPR018389. TRAP_DctP/TeaA.
[Graphical view]
PfamiPF03480. DctP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

E1VBK1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAYKLLTTA SIGALMLGMS TAAYSDNWRY AHEEYEGDVQ DVFAQAFKGY
60 70 80 90 100
VEDNSDHTVQ VYRFGELGES DDIMEQTQNG ILQFVNQSPG FTGSLIPSAQ
110 120 130 140 150
IFFIPYLMPT DMDTVLEFFD ESKAINEMFP KLYAEHGLEL LKMYPEGEMV
160 170 180 190 200
VTADEPITSP EDFDNKKIRT MTNPLLAETY KAFGATPTPL PWGEVYGGLQ
210 220 230 240 250
TGIIDGQENP IFWIESGGLY EVSPNLTFTS HGWFTTAMMA NQDFYEGLSE
260 270 280 290 300
EDQQLVQDAA DAAYDHTIEH IKGLSEESLE KIKAASDEVT VTRLNDEQIQ
310 320 330 340
AFKERAPQVE EKFIEMTGEQ GQELLDQFKA DLKAVQSESE G
Length:341
Mass (Da):38,265
Last modified:November 30, 2010 - v1
Checksum:iE632B3C8EA9E5A11
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY061646 Genomic DNA. Translation: AAL29684.1.
FN869568 Genomic DNA. Translation: CBV44158.1.
RefSeqiWP_013334028.1. NC_014532.1.

Genome annotation databases

EnsemblBacteriaiCBV44158; CBV44158; HELO_4274.
KEGGihel:HELO_4274.
PATRICi42358222. VBIHalElo161731_3511.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY061646 Genomic DNA. Translation: AAL29684.1.
FN869568 Genomic DNA. Translation: CBV44158.1.
RefSeqiWP_013334028.1. NC_014532.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VPNX-ray1.55A/B26-341[»]
2VPOX-ray1.80A/B26-341[»]
3GYYX-ray2.20A/B/C/D1-341[»]
ProteinModelPortaliE1VBK1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi768066.HELO_4274.

Protein family/group databases

TCDBi2.A.56.2.1. the tripartite atp-independent periplasmic transporter (trap-t) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCBV44158; CBV44158; HELO_4274.
KEGGihel:HELO_4274.
PATRICi42358222. VBIHalElo161731_3511.

Phylogenomic databases

eggNOGiENOG4108KJ1. Bacteria.
COG1638. LUCA.
HOGENOMiHOG000224244.
OMAiHEYQIRI.
OrthoDBiPOG091H03NF.

Enzyme and pathway databases

BioCyciHELO768066:GJEE-3356-MONOMER.

Family and domain databases

InterProiIPR018389. TRAP_DctP/TeaA.
[Graphical view]
PfamiPF03480. DctP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTEAA_HALED
AccessioniPrimary (citable) accession number: E1VBK1
Secondary accession number(s): Q8VPB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: November 30, 2010
Last modified: September 7, 2016
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The ectoine/TeaA complex displays a closed conformation (PubMed:18702523). Interaction with the transmembrane proteins induces opening of TeaA, which facilitates substrate release (PubMed:22084072).2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.