TSPO_CERSP
ID TSPO_CERSP Reviewed; 158 AA.
AC Q9RFC8;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Tryptophan-rich sensory protein {ECO:0000303|PubMed:7673149};
DE Short=TSPO {ECO:0000303|PubMed:10648776, ECO:0000303|PubMed:25635101};
DE AltName: Full=Translocator protein TspO {ECO:0000303|PubMed:23952237, ECO:0000303|PubMed:25635101};
DE AltName: Full=TspO regulatory protein {ECO:0000303|PubMed:10648776};
GN Name=tspO {ECO:0000303|PubMed:10648776, ECO:0000303|PubMed:7673149};
GN Synonyms=crtK {ECO:0000303|PubMed:7673149};
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063 {ECO:0000312|EMBL:AAF24291.1};
RN [1] {ECO:0000312|EMBL:AAF24291.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2.4.1 {ECO:0000312|EMBL:AAF24291.1};
RX PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA Choudhary M., Kaplan S.;
RT "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT sphaeroides 2.4.1.";
RL Nucleic Acids Res. 28:862-867(2000).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=2.4.1 {ECO:0000303|PubMed:7673149};
RX PubMed=7673149; DOI=10.1074/jbc.270.36.21167;
RA Yeliseev A.A., Kaplan S.;
RT "A sensory transducer homologous to the mammalian peripheral-type
RT benzodiazepine receptor regulates photosynthetic membrane complex formation
RT in Rhodobacter sphaeroides 2.4.1.";
RL J. Biol. Chem. 270:21167-21175(1995).
RN [3]
RP FUNCTION.
RC STRAIN=2.4.1 {ECO:0000303|PubMed:7673149};
RX PubMed=10409680; DOI=10.1074/jbc.274.30.21234;
RA Yeliseev A.A., Kaplan S.;
RT "A novel mechanism for the regulation of photosynthesis gene expression by
RT the TspO outer membrane protein of Rhodobacter sphaeroides 2.4.1.";
RL J. Biol. Chem. 274:21234-21243(1999).
RN [4]
RP FUNCTION, MUTAGENESIS OF CYS-15; TRP-30; TRP-38; TRP-39; TRP-44 AND TRP-50,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=2.4.1 {ECO:0000303|PubMed:7673149};
RX PubMed=10681549; DOI=10.1074/jbc.275.8.5657;
RA Yeliseev A.A., Kaplan S.;
RT "TspO of Rhodobacter sphaeroides. A structural and functional model for the
RT mammalian peripheral benzodiazepine receptor.";
RL J. Biol. Chem. 275:5657-5667(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23651039; DOI=10.1021/bi400364z;
RA Ginter C., Kiburu I., Boudker O.;
RT "Chemical catalysis by the translocator protein (18 kDa).";
RL Biochemistry 52:3609-3611(2013).
RN [6]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=2.4.1 {ECO:0000303|PubMed:23952237};
RX PubMed=23952237; DOI=10.1021/bi400431t;
RA Li F., Xia Y., Meiler J., Ferguson-Miller S.;
RT "Characterization and modeling of the oligomeric state and ligand binding
RT behavior of purified translocator protein 18 kDa from Rhodobacter
RT sphaeroides.";
RL Biochemistry 52:5884-5899(2013).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (10.2 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=20541505; DOI=10.1016/j.str.2010.03.001;
RA Korkhov V.M., Sachse C., Short J.M., Tate C.G.;
RT "Three-dimensional structure of TspO by electron cryomicroscopy of helical
RT crystals.";
RL Structure 18:677-687(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH PROTOPORPHYRIN IX,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF ALA-139.
RC STRAIN=2.4.1 {ECO:0000303|PubMed:25635101};
RX PubMed=25635101; DOI=10.1126/science.1260590;
RA Li F., Liu J., Zheng Y., Garavito R.M., Ferguson-Miller S.;
RT "Crystal structures of translocator protein (TSPO) and mutant mimic of a
RT human polymorphism.";
RL Science 347:555-558(2015).
CC -!- FUNCTION: May play a role in the transmembrane transport of
CC tetrapyrroles and similar compounds, and thereby contribute to the
CC regulation of tetrapyrrole biosynthesis (PubMed:10409680). Binds
CC tetrapyrroles and promotes the photooxidative degradation of
CC protoporphyrin IX (PubMed:23651039). Binds protoporphyrin IX, hemin,
CC and coproporphyrin III, but does not bind delta-aminolevulinic acid
CC (PubMed:23952237, PubMed:20541505, PubMed:25635101). Can bind
CC bilirubin, curcumin, gossypol, retinoic acid, cholesterol and the
CC benzodiazepine receptor agonist PK-11195 (in vitro) (PubMed:23952237,
CC PubMed:25635101). Plays a role in the response to low oxygen levels and
CC in the regulation of the biosynthesis of photosynthetic pigments
CC (PubMed:7673149, PubMed:10409680, PubMed:10681549).
CC {ECO:0000269|PubMed:10681549, ECO:0000269|PubMed:20541505,
CC ECO:0000269|PubMed:23651039, ECO:0000269|PubMed:23952237,
CC ECO:0000269|PubMed:25635101, ECO:0000269|PubMed:7673149,
CC ECO:0000305|PubMed:10409680}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10681549,
CC ECO:0000269|PubMed:20541505, ECO:0000269|PubMed:23952237,
CC ECO:0000269|PubMed:25635101}.
CC -!- INTERACTION:
CC Q9RFC8; Q9RFC8: tspO; NbExp=4; IntAct=EBI-15859752, EBI-15859752;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10681549,
CC ECO:0000269|PubMed:20541505, ECO:0000269|PubMed:23651039,
CC ECO:0000269|PubMed:23952237, ECO:0000269|PubMed:25635101,
CC ECO:0000269|PubMed:7673149}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20541505, ECO:0000269|PubMed:25635101}. Cell inner
CC membrane {ECO:0000305|PubMed:20541505}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20541505, ECO:0000269|PubMed:25635101}. Note=Outer
CC membrane proteins generally mediate transport processes by forming
CC beta-barrel structures, and unlike TspO, their transmembrane domains do
CC not contain any helices. Detected in the cell inner membrane when
CC expressed in E.coli (PubMed:20541505). This suggest that TspO is in the
CC inner membrane, even if experiments shown in PubMed:7673149 suggest
CC location in the outer membrane. {ECO:0000269|PubMed:20541505,
CC ECO:0000305}.
CC -!- INDUCTION: Up-regulated during photosynthetic growth, when compared to
CC aerobic growth in the dark (at protein level).
CC {ECO:0000269|PubMed:7673149}.
CC -!- DISRUPTION PHENOTYPE: No effect on chemoheterotrophic growth, and no
CC defects in the production of photosynthetic pigments. When oxygen
CC levels are reduced during chemoheterotrophic growth, mutant cells
CC respond more rapidly than wild-type and display faster accumulation of
CC carotenoids and bacteriochlorophylls. {ECO:0000269|PubMed:7673149}.
CC -!- SIMILARITY: Belongs to the TspO/BZRP family. {ECO:0000305}.
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DR EMBL; AF195122; AAF24291.1; -; Genomic_DNA.
DR PIR; A57438; A57438.
DR PDB; 4UC1; X-ray; 1.80 A; A/B/C=1-157.
DR PDB; 4UC2; X-ray; 2.40 A; A/B=2-157.
DR PDB; 4UC3; X-ray; 2.50 A; A/B=3-157.
DR PDB; 5DUO; X-ray; 2.40 A; A/B/C=1-157.
DR PDBsum; 4UC1; -.
DR PDBsum; 4UC2; -.
DR PDBsum; 4UC3; -.
DR PDBsum; 5DUO; -.
DR AlphaFoldDB; Q9RFC8; -.
DR SMR; Q9RFC8; -.
DR DIP; DIP-58981N; -.
DR OMA; CSWYRIN; -.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046906; F:tetrapyrrole binding; IDA:UniProtKB.
DR GO; GO:0033013; P:tetrapyrrole metabolic process; IDA:UniProtKB.
DR CDD; cd15904; TSPO_MBR; 1.
DR Gene3D; 1.20.1260.100; -; 1.
DR InterPro; IPR038330; TspO/MBR-related_sf.
DR InterPro; IPR004307; TspO_MBR.
DR PANTHER; PTHR10057; PTHR10057; 1.
DR Pfam; PF03073; TspO_MBR; 1.
DR PIRSF; PIRSF005859; PBR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Lipid-binding; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..158
FT /note="Tryptophan-rich sensory protein"
FT /id="PRO_0000432576"
FT TRANSMEM 5..25
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:25635101"
FT TRANSMEM 44..65
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:25635101"
FT TRANSMEM 73..93
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:25635101"
FT TRANSMEM 97..119
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:25635101"
FT TRANSMEM 124..144
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:25635101"
FT MUTAGEN 15
FT /note="C->S: Leads to decreased levels of the protein and
FT increased levels of carotenoids and bacteriochlorophylls."
FT /evidence="ECO:0000269|PubMed:10681549"
FT MUTAGEN 30
FT /note="W->F: Slightly increased levels of carotenoids and
FT bacteriochlorophylls."
FT /evidence="ECO:0000269|PubMed:10681549"
FT MUTAGEN 38
FT /note="W->C: Decreases growth rate 2-3 fold. Leads to
FT increased levels of the protein and decreased levels of
FT carotenoids and bacteriochlorophylls."
FT /evidence="ECO:0000269|PubMed:10681549"
FT MUTAGEN 39
FT /note="W->F: Increased levels of carotenoids and
FT bacteriochlorophylls."
FT /evidence="ECO:0000269|PubMed:10681549"
FT MUTAGEN 44
FT /note="W->F: Increased levels of carotenoids and
FT bacteriochlorophylls."
FT /evidence="ECO:0000269|PubMed:10681549"
FT MUTAGEN 50
FT /note="W->F: Increased levels of carotenoids and
FT bacteriochlorophylls."
FT /evidence="ECO:0000269|PubMed:10681549"
FT MUTAGEN 139
FT /note="A->T: Decreases affinity for protoporphyrin IX,
FT cholesterol and the benzodiazepine receptor agonist PK-
FT 11195."
FT /evidence="ECO:0000269|PubMed:25635101"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:4UC1"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:4UC1"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:4UC1"
FT HELIX 45..64
FT /evidence="ECO:0007829|PDB:4UC1"
FT HELIX 71..92
FT /evidence="ECO:0007829|PDB:4UC1"
FT HELIX 97..119
FT /evidence="ECO:0007829|PDB:4UC1"
FT HELIX 123..148
FT /evidence="ECO:0007829|PDB:4UC1"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:4UC2"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:4UC3"
SQ SEQUENCE 158 AA; 17976 MW; 16569B7156AFD0CD CRC64;
MNMDWALFLT FLAACGAPAT TGALLKPDEW YDNLNKPWWN PPRWVFPLAW TSLYFLMSLA
AMRVAQLEGS GQALAFYAAQ LAFNTLWTPV FFGMKRMATA LAVVMVMWLF VAATMWAFFQ
LDTWAGVLFV PYLIWATAAT GLNFEAMRLN WNRPEARA
