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Tryptophan-rich sensory protein (TSPO) (Translocator protein TspO) (TspO regulatory protein)

 TSPO_RHOSH              Reviewed;         158 AA.
Q9RFC8;
01-APR-2015, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-MAR-2018, entry version 40.
RecName: Full=Tryptophan-rich sensory protein {ECO:0000303|PubMed:7673149};
Short=TSPO {ECO:0000303|PubMed:10648776, ECO:0000303|PubMed:25635101};
AltName: Full=Translocator protein TspO {ECO:0000303|PubMed:23952237, ECO:0000303|PubMed:25635101};
AltName: Full=TspO regulatory protein {ECO:0000303|PubMed:10648776};
Name=tspO {ECO:0000303|PubMed:10648776, ECO:0000303|PubMed:7673149};
Synonyms=crtK {ECO:0000303|PubMed:7673149};
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Rhodobacter.
NCBI_TaxID=1063 {ECO:0000312|EMBL:AAF24291.1};
[1] {ECO:0000312|EMBL:AAF24291.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=2.4.1 {ECO:0000312|EMBL:AAF24291.1};
PubMed=10648776; DOI=10.1093/nar/28.4.862;
Choudhary M., Kaplan S.;
"DNA sequence analysis of the photosynthesis region of Rhodobacter
sphaeroides 2.4.1.";
Nucleic Acids Res. 28:862-867(2000).
[2]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INDUCTION.
STRAIN=2.4.1 {ECO:0000303|PubMed:7673149};
PubMed=7673149; DOI=10.1074/jbc.270.36.21167;
Yeliseev A.A., Kaplan S.;
"A sensory transducer homologous to the mammalian peripheral-type
benzodiazepine receptor regulates photosynthetic membrane complex
formation in Rhodobacter sphaeroides 2.4.1.";
J. Biol. Chem. 270:21167-21175(1995).
[3]
FUNCTION.
STRAIN=2.4.1 {ECO:0000303|PubMed:7673149};
PubMed=10409680; DOI=10.1074/jbc.274.30.21234;
Yeliseev A.A., Kaplan S.;
"A novel mechanism for the regulation of photosynthesis gene
expression by the TspO outer membrane protein of Rhodobacter
sphaeroides 2.4.1.";
J. Biol. Chem. 274:21234-21243(1999).
[4]
FUNCTION, MUTAGENESIS OF CYS-15; TRP-30; TRP-38; TRP-39; TRP-44 AND
TRP-50, SUBCELLULAR LOCATION, AND SUBUNIT.
STRAIN=2.4.1 {ECO:0000303|PubMed:7673149};
PubMed=10681549; DOI=10.1074/jbc.275.8.5657;
Yeliseev A.A., Kaplan S.;
"TspO of Rhodobacter sphaeroides. A structural and functional model
for the mammalian peripheral benzodiazepine receptor.";
J. Biol. Chem. 275:5657-5667(2000).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23651039; DOI=10.1021/bi400364z;
Ginter C., Kiburu I., Boudker O.;
"Chemical catalysis by the translocator protein (18 kDa).";
Biochemistry 52:3609-3611(2013).
[6]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=2.4.1 {ECO:0000303|PubMed:23952237};
PubMed=23952237; DOI=10.1021/bi400431t;
Li F., Xia Y., Meiler J., Ferguson-Miller S.;
"Characterization and modeling of the oligomeric state and ligand
binding behavior of purified translocator protein 18 kDa from
Rhodobacter sphaeroides.";
Biochemistry 52:5884-5899(2013).
[7]
STRUCTURE BY ELECTRON MICROSCOPY (10.2 ANGSTROMS), FUNCTION,
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=20541505; DOI=10.1016/j.str.2010.03.001;
Korkhov V.M., Sachse C., Short J.M., Tate C.G.;
"Three-dimensional structure of TspO by electron cryomicroscopy of
helical crystals.";
Structure 18:677-687(2010).
[8]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH PROTOPORPHYRIN
IX, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF
ALA-139.
STRAIN=2.4.1 {ECO:0000303|PubMed:25635101};
PubMed=25635101; DOI=10.1126/science.1260590;
Li F., Liu J., Zheng Y., Garavito R.M., Ferguson-Miller S.;
"Crystal structures of translocator protein (TSPO) and mutant mimic of
a human polymorphism.";
Science 347:555-558(2015).
-!- FUNCTION: May play a role in the transmembrane transport of
tetrapyrroles and similar compounds, and thereby contribute to the
regulation of tetrapyrrole biosynthesis (PubMed:10409680). Binds
tetrapyrroles and promotes the photooxidative degradation of
protoporphyrin IX (PubMed:23651039). Binds protoporphyrin IX,
hemin, and coproporphyrin III, but does not bind delta-
aminolevulinic acid (PubMed:23952237, PubMed:20541505,
PubMed:25635101). Can bind bilirubin, curcumin, gossypol, retinoic
acid, cholesterol and the benzodiazepine receptor agonist PK-11195
(in vitro) (PubMed:23952237, PubMed:25635101). Plays a role in the
response to low oxygen levels and in the regulation of the
biosynthesis of photosynthetic pigments (PubMed:7673149,
PubMed:10409680, PubMed:10681549). {ECO:0000269|PubMed:10681549,
ECO:0000269|PubMed:20541505, ECO:0000269|PubMed:23651039,
ECO:0000269|PubMed:23952237, ECO:0000269|PubMed:25635101,
ECO:0000269|PubMed:7673149, ECO:0000305|PubMed:10409680}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10681549,
ECO:0000269|PubMed:20541505, ECO:0000269|PubMed:23952237,
ECO:0000269|PubMed:25635101}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-15859752, EBI-15859752;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10681549,
ECO:0000269|PubMed:20541505, ECO:0000269|PubMed:23651039,
ECO:0000269|PubMed:23952237, ECO:0000269|PubMed:25635101,
ECO:0000269|PubMed:7673149}; Multi-pass membrane protein
{ECO:0000269|PubMed:20541505, ECO:0000269|PubMed:25635101}. Cell
inner membrane {ECO:0000305|PubMed:20541505}; Multi-pass membrane
protein {ECO:0000269|PubMed:20541505,
ECO:0000269|PubMed:25635101}. Note=Outer membrane proteins
generally mediate transport processes by forming beta-barrel
structures, and unlike TspO, their transmembrane domains do not
contain any helices. Detected in the cell inner membrane when
expressed in E.coli (PubMed:20541505). This suggest that TspO is
in the inner membrane, even if experiments shown in PubMed:7673149
suggest location in the outer membrane.
{ECO:0000269|PubMed:20541505, ECO:0000305}.
-!- INDUCTION: Up-regulated during photosynthetic growth, when
compared to aerobic growth in the dark (at protein level).
{ECO:0000269|PubMed:7673149}.
-!- DISRUPTION PHENOTYPE: No effect on chemoheterotrophic growth, and
no defects in the production of photosynthetic pigments. When
oxygen levels are reduced during chemoheterotrophic growth, mutant
cells respond more rapidly than wild-type and display faster
accumulation of carotenoids and bacteriochlorophylls.
{ECO:0000269|PubMed:7673149}.
-!- SIMILARITY: Belongs to the TspO/BZRP family. {ECO:0000305}.
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EMBL; AF195122; AAF24291.1; -; Genomic_DNA.
PIR; A57438; A57438.
PDB; 4UC1; X-ray; 1.80 A; A/B/C=1-157.
PDB; 4UC2; X-ray; 2.40 A; A/B=2-157.
PDB; 4UC3; X-ray; 2.50 A; A/B=3-157.
PDB; 5DUO; X-ray; 2.40 A; A/B/C=1-157.
PDBsum; 4UC1; -.
PDBsum; 4UC2; -.
PDBsum; 4UC3; -.
PDBsum; 5DUO; -.
SMR; Q9RFC8; -.
DIP; DIP-58981N; -.
eggNOG; ENOG4105KAV; Bacteria.
eggNOG; COG3476; LUCA.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046906; F:tetrapyrrole binding; IDA:UniProtKB.
GO; GO:0033013; P:tetrapyrrole metabolic process; IDA:UniProtKB.
CDD; cd15904; TSPO_MBR; 1.
Gene3D; 1.20.1260.100; -; 1.
InterPro; IPR038330; TspO/MBR-related_sf.
InterPro; IPR004307; TspO_MBR.
PANTHER; PTHR10057; PTHR10057; 1.
Pfam; PF03073; TspO_MBR; 1.
PIRSF; PIRSF005859; PBR; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Lipid-binding;
Membrane; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 158 Tryptophan-rich sensory protein.
/FTId=PRO_0000432576.
TRANSMEM 5 25 Helical; Name=1.
{ECO:0000269|PubMed:25635101}.
TRANSMEM 44 65 Helical; Name=2.
{ECO:0000269|PubMed:25635101}.
TRANSMEM 73 93 Helical; Name=3.
{ECO:0000269|PubMed:25635101}.
TRANSMEM 97 119 Helical; Name=4.
{ECO:0000269|PubMed:25635101}.
TRANSMEM 124 144 Helical; Name=5.
{ECO:0000269|PubMed:25635101}.
MUTAGEN 15 15 C->S: Leads to decreased levels of the
protein and increased levels of
carotenoids and bacteriochlorophylls.
{ECO:0000269|PubMed:10681549}.
MUTAGEN 30 30 W->F: Slightly increased levels of
carotenoids and bacteriochlorophylls.
{ECO:0000269|PubMed:10681549}.
MUTAGEN 38 38 W->C: Decreases growth rate 2-3 fold.
Leads to increased levels of the protein
and decreased levels of carotenoids and
bacteriochlorophylls.
{ECO:0000269|PubMed:10681549}.
MUTAGEN 39 39 W->F: Increased levels of carotenoids and
bacteriochlorophylls.
{ECO:0000269|PubMed:10681549}.
MUTAGEN 44 44 W->F: Increased levels of carotenoids and
bacteriochlorophylls.
{ECO:0000269|PubMed:10681549}.
MUTAGEN 50 50 W->F: Increased levels of carotenoids and
bacteriochlorophylls.
{ECO:0000269|PubMed:10681549}.
MUTAGEN 139 139 A->T: Decreases affinity for
protoporphyrin IX, cholesterol and the
benzodiazepine receptor agonist PK-11195.
{ECO:0000269|PubMed:25635101}.
HELIX 5 14 {ECO:0000244|PDB:4UC1}.
HELIX 16 23 {ECO:0000244|PDB:4UC1}.
HELIX 29 33 {ECO:0000244|PDB:4UC1}.
HELIX 45 64 {ECO:0000244|PDB:4UC1}.
HELIX 71 92 {ECO:0000244|PDB:4UC1}.
HELIX 97 119 {ECO:0000244|PDB:4UC1}.
HELIX 123 148 {ECO:0000244|PDB:4UC1}.
TURN 150 152 {ECO:0000244|PDB:4UC2}.
TURN 154 156 {ECO:0000244|PDB:4UC3}.
SEQUENCE 158 AA; 17976 MW; 16569B7156AFD0CD CRC64;
MNMDWALFLT FLAACGAPAT TGALLKPDEW YDNLNKPWWN PPRWVFPLAW TSLYFLMSLA
AMRVAQLEGS GQALAFYAAQ LAFNTLWTPV FFGMKRMATA LAVVMVMWLF VAATMWAFFQ
LDTWAGVLFV PYLIWATAAT GLNFEAMRLN WNRPEARA


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