UEHA_RUEPO
ID UEHA_RUEPO Reviewed; 339 AA.
AC Q5LUA7;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ectoine/5-hydroxyectoine-binding periplasmic protein UehA {ECO:0000305};
DE AltName: Full=Uptake of ectoine and hydroxyectoine protein A {ECO:0000305};
DE Flags: Precursor;
GN Name=uehA {ECO:0000303|PubMed:19362561};
GN OrderedLocusNames=SPO1147 {ECO:0000312|EMBL:AAV94447.1};
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
RN [3] {ECO:0007744|PDB:3FXB}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 28-339 IN COMPLEX WITH ECTOINE,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISULFIDE BOND.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=19362561; DOI=10.1016/j.jmb.2009.03.077;
RA Lecher J., Pittelkow M., Zobel S., Bursy J., Bonig T., Smits S.H.,
RA Schmitt L., Bremer E.;
RT "The crystal structure of UehA in complex with ectoine-A comparison with
RT other TRAP-T binding proteins.";
RL J. Mol. Biol. 389:58-73(2009).
CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system UehABC, which imports both ectoine and 5-
CC hydroxyectoine as nutrients, and not as osmoprotectants. UehA binds
CC both ectoine and 5-hydroxyectoine with high specificity and affinity.
CC {ECO:0000269|PubMed:19362561}.
CC -!- SUBUNIT: Monomer (PubMed:19362561). The complex comprises the
CC extracytoplasmic solute receptor protein UehA, and the two
CC transmembrane proteins UehB and UehC (Probable).
CC {ECO:0000269|PubMed:19362561, ECO:0000305|PubMed:19362561}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:19362561}.
CC -!- MISCELLANEOUS: Transport is enhanced in cells that are grown in the
CC presence of ectoine, but not by high-salinity media.
CC {ECO:0000269|PubMed:19362561}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC {ECO:0000305}.
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DR EMBL; CP000031; AAV94447.1; -; Genomic_DNA.
DR RefSeq; WP_011046894.1; NC_003911.12.
DR PDB; 3FXB; X-ray; 2.90 A; A/B=28-339.
DR PDBsum; 3FXB; -.
DR AlphaFoldDB; Q5LUA7; -.
DR SMR; Q5LUA7; -.
DR STRING; 246200.SPO1147; -.
DR EnsemblBacteria; AAV94447; AAV94447; SPO1147.
DR KEGG; sil:SPO1147; -.
DR eggNOG; COG1638; Bacteria.
DR HOGENOM; CLU_036176_1_0_5; -.
DR OMA; KAINEMF; -.
DR OrthoDB; 752834at2; -.
DR EvolutionaryTrace; Q5LUA7; -.
DR Proteomes; UP000001023; 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; Disulfide bond; Periplasm; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..339
FT /note="Ectoine/5-hydroxyectoine-binding periplasmic protein
FT UehA"
FT /id="PRO_5004259469"
FT BINDING 36
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT /evidence="ECO:0000269|PubMed:19362561"
FT BINDING 171
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT /evidence="ECO:0000269|PubMed:19362561"
FT BINDING 211
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT /evidence="ECO:0000269|PubMed:19362561"
FT BINDING 215
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT /evidence="ECO:0000269|PubMed:19362561"
FT BINDING 236
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT /evidence="ECO:0000269|PubMed:19362561"
FT DISULFID 162..303
FT /evidence="ECO:0000269|PubMed:19362561"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 41..55
FT /evidence="ECO:0007829|PDB:3FXB"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3FXB"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:3FXB"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3FXB"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:3FXB"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:3FXB"
FT STRAND 140..157
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3FXB"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:3FXB"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:3FXB"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:3FXB"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:3FXB"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 252..277
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:3FXB"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:3FXB"
FT HELIX 298..335
FT /evidence="ECO:0007829|PDB:3FXB"
SQ SEQUENCE 339 AA; 37276 MW; 174B38DFCC11354E CRC64;
MAQSITFTFG AVAAAGIALA AGTAAQADTW RYAFEEAMTD VQGVYAQKFK EEIEANSDHE
IQLFPYGTLG ESADIMEQTQ DGILQFVDQS PGFTGSLIPE AQVFFVPYLL PTDQDHLARF
FKESKAINDM FKPLYADQGL ELLNMFPEGE VAMTTKTPVT TCSDLDEVKF RVMTNPLLVE
SYKAFGATPT PLPWGEVYGG LQTNVIQGQE NPTFFLYSTK IYEVTDYITY AGHNNFTTAV
MANKDFYDGL SAEDQQLVQN AALAAYDHTV VYQQQAADTE LAKIMEAKPE MQVTVLTDEQ
RSCFKEAAAE VEAKFIEMTG DSGAAILKQM KADLAATAN
