TSPO_CHLTE
ID TSPO_CHLTE Reviewed; 158 AA.
AC Q8KBX2;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Tryptophan-rich protein TspO {ECO:0000305};
DE AltName: Full=Translocator protein TspO {ECO:0000303|PubMed:23651039};
GN Name=crtK-2 {ECO:0000312|EMBL:AAM72885.1}; Synonyms=tspO;
GN OrderedLocusNames=CT1660 {ECO:0000312|EMBL:AAM72885.1};
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439 {ECO:0000312|EMBL:AAM72885.1};
RN [1] {ECO:0000312|EMBL:AAM72885.1, ECO:0000312|Proteomes:UP000001007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
RC {ECO:0000312|Proteomes:UP000001007};
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-142 AND ALA-146.
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).
CC -!- FUNCTION: Binds tetrapyrroles and promotes the photooxidative
CC degradation of protoporphyrin IX (PubMed:23651039). Can bind the
CC benzodiazepine receptor agonist PK-11195 (in vitro); this interferes
CC with photooxidative tetrapyrrole degradation (PubMed:23651039). May
CC play a role in the transmembrane transport of tetrapyrroles and similar
CC compounds (By similarity). {ECO:0000250|UniProtKB:Q9RFC8,
CC ECO:0000269|PubMed:23651039}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:23651039}; Multi-
CC pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TspO/BZRP family. {ECO:0000305}.
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DR EMBL; AE006470; AAM72885.1; -; Genomic_DNA.
DR RefSeq; NP_662543.1; NC_002932.3.
DR RefSeq; WP_010933324.1; NC_002932.3.
DR AlphaFoldDB; Q8KBX2; -.
DR SMR; Q8KBX2; -.
DR STRING; 194439.CT1660; -.
DR EnsemblBacteria; AAM72885; AAM72885; CT1660.
DR KEGG; cte:CT1660; -.
DR eggNOG; COG3476; Bacteria.
DR HOGENOM; CLU_091805_2_0_10; -.
DR OMA; GLNLIWM; -.
DR OrthoDB; 1679387at2; -.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..158
FT /note="Tryptophan-rich protein TspO"
FT /id="PRO_0000432575"
FT TRANSMEM 5..25
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT MUTAGEN 142
FT /note="W->F: No effect on protoporphyrin IX binding. Nearly
FT abolishes protoporphyrin IX photooxidation."
FT /evidence="ECO:0000269|PubMed:23651039"
FT MUTAGEN 146
FT /note="A->T: Decreases affinity for protoporphyrin IX.
FT Nearly abolishes protoporphyrin IX photooxidation."
FT /evidence="ECO:0000269|PubMed:23651039"
SQ SEQUENCE 158 AA; 17506 MW; E66D1272677A476A CRC64;
MNKQILTLAL CIGLCLAVGF AGSTFTPKPA SWYYTTLVKP SWNPPDWLFP PVWTILFIMM
GTALAKVLGT GWKKNEVNVG VVLFAIQLML NLGWSASFFG MQSPLAGLVD IVLLWIFIVL
TMLAFARVSK PASLLLVPYL CWVSFASYLN FTILQLNP
