ID   TEAD_HALED              Reviewed;         147 AA.
AC   E1VBK4; D2TGC1; D4AEP4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=TRAP-T-associated universal stress protein TeaD;
DE   AltName: Full=UspA domain transporter regulator TeaD;
GN   Name=teaD; OrderedLocusNames=HELO_4277;
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, INDUCTION, DISRUPTION
RP   PHENOTYPE, AND X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ATP.
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX   PubMed=20113006; DOI=10.1021/bi9017522;
RA   Schweikhard E.S., Kuhlmann S.I., Kunte H.J., Grammann K., Ziegler C.M.;
RT   "Structure and function of the universal stress protein TeaD and its role
RT   in regulating the ectoine transporter TeaABC of Halomonas elongata DSM
RT   2581(T).";
RL   Biochemistry 49:2194-2204(2010).
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).
CC   -!- FUNCTION: ATP-binding protein that negatively regulates activity of the
CC       tripartite ATP-independent periplasmic (TRAP) ectoine transport system
CC       TeaABC. May regulate uptake according to the ATP status of the cell.
CC       {ECO:0000269|PubMed:20113006}.
CC   -!- SUBUNIT: Homodimer or homotetramer; in equilibrium. The dimer/tetramer
CC       ratio is ATP-dependent. ATP stabilizes dimer-dimer complexes, with one
CC       ATP molecule bound to each monomer. {ECO:0000269|PubMed:20113006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Cotranscribed along with teaABC.
CC       {ECO:0000269|PubMed:20113006}.
CC   -!- DISRUPTION PHENOTYPE: Deletion results in an enhanced uptake for
CC       ectoine by TeaABC. {ECO:0000269|PubMed:20113006}.
CC   -!- SIMILARITY: Belongs to the universal stress protein A family.
CC       {ECO:0000305}.
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DR   EMBL; FN435983; CBA13558.1; -; Genomic_DNA.
DR   EMBL; FN869568; CBV44161.1; -; Genomic_DNA.
DR   RefSeq; WP_013334031.1; NC_014532.2.
DR   PDB; 3HGM; X-ray; 1.90 A; A/B/C/D=1-147.
DR   PDBsum; 3HGM; -.
DR   AlphaFoldDB; E1VBK4; -.
DR   SMR; E1VBK4; -.
DR   STRING; 768066.HELO_4277; -.
DR   EnsemblBacteria; CBV44161; CBV44161; HELO_4277.
DR   KEGG; hel:HELO_4277; -.
DR   eggNOG; COG0589; Bacteria.
DR   HOGENOM; CLU_049301_11_0_6; -.
DR   OMA; HSLFEAS; -.
DR   Proteomes; UP000008707; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR006015; Universal_stress_UspA.
DR   InterPro; IPR006016; UspA.
DR   Pfam; PF00582; Usp; 1.
DR   PRINTS; PR01438; UNVRSLSTRESS.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..147
FT                   /note="TRAP-T-associated universal stress protein TeaD"
FT                   /id="PRO_0000428827"
FT   BINDING         8..10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:20113006"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:20113006"
FT   BINDING         117..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:20113006"
FT   BINDING         131..133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:20113006"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   HELIX           13..29
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   STRAND          32..39
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   HELIX           42..47
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   HELIX           63..81
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   STRAND          89..96
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   HELIX           98..108
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   STRAND          112..119
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   HELIX           131..139
FT                   /evidence="ECO:0007829|PDB:3HGM"
FT   STRAND          144..147
FT                   /evidence="ECO:0007829|PDB:3HGM"
SQ   SEQUENCE   147 AA;  15751 MW;  3506DB4E2A8ED29C CRC64;
     MFNRIMVPVD GSKGAVKALE KGVGLQQLTG AELYILCVFK HHSLLEASLS MVRPEQLDIP
     DDALKDYATE IAVQAKTRAT ELGVPADKVR AFVKGGRPSR TIVRFARKRE CDLVVIGAQG
     TNGDKSLLLG SVAQRVAGSA HCPVLVV