TEAA_HALED
ID TEAA_HALED Reviewed; 341 AA.
AC E1VBK1; Q8VPB3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Ectoine-binding periplasmic protein TeaA;
DE Flags: Precursor;
GN Name=teaA; OrderedLocusNames=HELO_4274;
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE,
RP AND GENE NAME.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=12003950; DOI=10.1128/jb.184.11.3078-3085.2002;
RA Grammann K., Volke A., Kunte H.J.;
RT "New type of osmoregulated solute transporter identified in halophilic
RT members of the bacteria domain: TRAP transporter TeaABC mediates uptake of
RT ectoine and hydroxyectoine in Halomonas elongata DSM 2581(T).";
RL J. Bacteriol. 184:3078-3085(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
RN [3]
RP PROTEIN SEQUENCE OF 26-35, FUNCTION AS A SUBSTRATE-BINDING PROTEIN, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=12076815; DOI=10.1111/j.1574-6968.2002.tb11227.x;
RA Tetsch L., Kunte H.J.;
RT "The substrate-binding protein TeaA of the osmoregulated ectoine
RT transporter TeaABC from Halomonas elongata: purification and
RT characterization of recombinant TeaA.";
RL FEMS Microbiol. Lett. 211:213-218(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 26-341 IN COMPLEXES WITH ECTOINE
RP AND HYDROXYECTOINE, FUNCTION AS A SUBSTRATE-BINDING PROTEIN, AND SUBUNIT.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=18702523; DOI=10.1021/bi8006719;
RA Kuhlmann S.I., Terwisscha van Scheltinga A.C., Bienert R., Kunte H.J.,
RA Ziegler C.;
RT "1.55 A structure of the ectoine binding protein TeaA of the osmoregulated
RT TRAP-transporter TeaABC from Halomonas elongata.";
RL Biochemistry 47:9475-9485(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), ALLOSTERIC REGULATION, AND
RP MUTAGENESIS OF GLY-273 AND 273-GLY--SER-275.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=22084072; DOI=10.1073/pnas.1112534108;
RA Marinelli F., Kuhlmann S.I., Grell E., Kunte H.J., Ziegler C.,
RA Faraldo-Gomez J.D.;
RT "Evidence for an allosteric mechanism of substrate release from membrane-
RT transporter accessory binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:E1285-E1292(2011).
CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system TeaABC involved in the uptake of ectoine and
CC hydroxyectoine in response to osmotic upshock. Probably functions as a
CC recovery system for synthesized ectoine that leaks out of the cell.
CC Binds ectoine with high affinity. Affinity for hydroxyectoine is
CC approximately 20-fold lower. {ECO:0000269|PubMed:12003950,
CC ECO:0000269|PubMed:12076815, ECO:0000269|PubMed:18702523}.
CC -!- SUBUNIT: Monomer. The complex comprises the extracytoplasmic solute
CC receptor protein TeaA, and the two transmembrane proteins TeaB and
CC TeaC. {ECO:0000269|PubMed:12003950, ECO:0000269|PubMed:18702523}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:12076815}.
CC -!- DISRUPTION PHENOTYPE: Deletion abolishes accumulation of ectoine from
CC the medium. {ECO:0000269|PubMed:12003950}.
CC -!- MISCELLANEOUS: The ectoine/TeaA complex displays a closed conformation
CC (PubMed:18702523). Interaction with the transmembrane proteins induces
CC opening of TeaA, which facilitates substrate release (PubMed:22084072).
CC {ECO:0000305|PubMed:18702523, ECO:0000305|PubMed:22084072}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC {ECO:0000305}.
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DR EMBL; AY061646; AAL29684.1; -; Genomic_DNA.
DR EMBL; FN869568; CBV44158.1; -; Genomic_DNA.
DR PDB; 2VPN; X-ray; 1.55 A; A/B=26-341.
DR PDB; 2VPO; X-ray; 1.80 A; A/B=26-341.
DR PDB; 3GYY; X-ray; 2.20 A; A/B/C/D=1-341.
DR PDBsum; 2VPN; -.
DR PDBsum; 2VPO; -.
DR PDBsum; 3GYY; -.
DR AlphaFoldDB; E1VBK1; -.
DR SMR; E1VBK1; -.
DR STRING; 768066.HELO_4274; -.
DR TCDB; 2.A.56.1.11; the tripartite atp-independent periplasmic transporter (trap-t) family.
DR EnsemblBacteria; CBV44158; CBV44158; HELO_4274.
DR KEGG; hel:HELO_4274; -.
DR eggNOG; COG1638; Bacteria.
DR HOGENOM; CLU_036176_1_0_6; -.
DR OMA; KAINEMF; -.
DR Proteomes; UP000008707; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0071702; P:organic substance transport; IEA:UniProt.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.40.190.170; -; 1.
DR InterPro; IPR018389; DctP_fam.
DR InterPro; IPR038404; TRAP_DctP_sf.
DR PANTHER; PTHR33376; PTHR33376; 1.
DR Pfam; PF03480; DctP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Periplasm; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:12076815"
FT CHAIN 26..341
FT /note="Ectoine-binding periplasmic protein TeaA"
FT /id="PRO_0000428828"
FT BINDING 34
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT BINDING 169
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT BINDING 209
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT BINDING 213
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT BINDING 234
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT MUTAGEN 273..275
FT /note="GLS->AAA: Strongly biased toward the open
FT conformation. Has lower affinity for ectoine. Does not
FT affect the structure of the substrate-binding site."
FT /evidence="ECO:0000269|PubMed:22084072"
FT MUTAGEN 273
FT /note="G->P: Conformationally unbiased. Has wild-type
FT affinity for ectoine."
FT /evidence="ECO:0000269|PubMed:22084072"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:2VPN"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2VPN"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2VPN"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:3GYY"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:2VPN"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:2VPN"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:2VPN"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:2VPN"
FT STRAND 138..155
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:2VPN"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:2VPN"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:2VPN"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:2VPN"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:2VPN"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 250..271
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 274..285
FT /evidence="ECO:0007829|PDB:2VPN"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:2VPN"
FT HELIX 306..334
FT /evidence="ECO:0007829|PDB:2VPN"
SQ SEQUENCE 341 AA; 38265 MW; E632B3C8EA9E5A11 CRC64;
MKAYKLLTTA SIGALMLGMS TAAYSDNWRY AHEEYEGDVQ DVFAQAFKGY VEDNSDHTVQ
VYRFGELGES DDIMEQTQNG ILQFVNQSPG FTGSLIPSAQ IFFIPYLMPT DMDTVLEFFD
ESKAINEMFP KLYAEHGLEL LKMYPEGEMV VTADEPITSP EDFDNKKIRT MTNPLLAETY
KAFGATPTPL PWGEVYGGLQ TGIIDGQENP IFWIESGGLY EVSPNLTFTS HGWFTTAMMA
NQDFYEGLSE EDQQLVQDAA DAAYDHTIEH IKGLSEESLE KIKAASDEVT VTRLNDEQIQ
AFKERAPQVE EKFIEMTGEQ GQELLDQFKA DLKAVQSESE G
