ID   TSPO_ARCFU              Reviewed;         153 AA.
AC   O28797;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Tryptophan-rich protein TspO {ECO:0000305};
DE   AltName: Full=Translocator protein TspO {ECO:0000303|PubMed:23651039};
GN   Name=tspO; OrderedLocusNames=AF_1475 {ECO:0000312|EMBL:AAB89774.1};
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325 {ECO:0000312|Proteomes:UP000002199};
RN   [1] {ECO:0000312|EMBL:AAB89774.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16
RC   {ECO:0000312|Proteomes:UP000002199};
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
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).
CC   -!- FUNCTION: Binds tetrapyrroles and promotes the photooxidative
CC       degradation of protoporphyrin IX (PubMed:23651039). May play a role in
CC       the transmembrane transport of tetrapyrroles and similar compounds (By
CC       similarity). {ECO:0000250|UniProtKB:Q9RFC8,
CC       ECO:0000269|PubMed:23651039}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TspO/BZRP family. {ECO:0000305}.
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DR   EMBL; AE000782; AAB89774.1; -; Genomic_DNA.
DR   PIR; B69434; B69434.
DR   RefSeq; WP_010878972.1; NC_000917.1.
DR   AlphaFoldDB; O28797; -.
DR   SMR; O28797; -.
DR   STRING; 224325.AF_1475; -.
DR   DNASU; 1484701; -.
DR   EnsemblBacteria; AAB89774; AAB89774; AF_1475.
DR   GeneID; 24795224; -.
DR   KEGG; afu:AF_1475; -.
DR   eggNOG; arCOG04434; Archaea.
DR   HOGENOM; CLU_091805_2_0_2; -.
DR   OMA; GLNLIWM; -.
DR   OrthoDB; 95433at2157; -.
DR   PhylomeDB; O28797; -.
DR   Proteomes; UP000002199; 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   3: Inferred from homology;
KW   Cell membrane; Membrane; Receptor; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..153
FT                   /note="Tryptophan-rich protein TspO"
FT                   /id="PRO_0000432573"
FT   TRANSMEM        3..23
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   153 AA;  17185 MW;  45E092270F9ED73E CRC64;
     MNILKLVASI LAVLAIGFAG SFFTAQSVQT WYAGVEKPFF TPPNWLFGPA WTLLYFLIGI
     VLYIAWENGF WNDSRVKATF FTQLGLNFLW SILFFGLQNP LAGLVDIIAL DIAVILTIVY
     IYHHSKASLL LLPYLGWILF ASALNFAIYL LNA