TSPO_BACCR
ID TSPO_BACCR Reviewed; 153 AA.
AC Q81BL7;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Tryptophan-rich protein TspO {ECO:0000305};
GN Name=tspO; OrderedLocusNames=BC_3136 {ECO:0000312|EMBL:AAP10078.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000312|EMBL:AAP10078.1};
RN [1] {ECO:0000312|EMBL:AAP10078.1, ECO:0000312|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711 {ECO:0000312|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH PK11195, FUNCTION,
RP SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF TRP-51; TRP-138 AND
RP ALA-142.
RX PubMed=25635100; DOI=10.1126/science.aaa1534;
RA Guo Y., Kalathur R.C., Liu Q., Kloss B., Bruni R., Ginter C., Kloppmann E.,
RA Rost B., Hendrickson W.A.;
RT "Structure and activity of tryptophan-rich TSPO proteins.";
RL Science 347:551-555(2015).
CC -!- FUNCTION: Binds tetrapyrroles and promotes the photooxidative
CC degradation of protoporphyrin IX (PubMed:25635100). Can bind the
CC benzodiazepine receptor agonist PK-11195 (in vitro); this interferes
CC with photooxidative tetrapyrrole degradation (PubMed:25635100). 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:25635100}.
CC -!- SUBUNIT: Monomer and homodimer. May also form higher oligomers.
CC {ECO:0000269|PubMed:25635100}.
CC -!- INTERACTION:
CC Q81BL7; Q81BL7: tspO; NbExp=2; IntAct=EBI-16140888, EBI-16140888;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:25635100}. Membrane
CC {ECO:0000269|PubMed:25635100}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:25635100}.
CC -!- SIMILARITY: Belongs to the TspO/BZRP family. {ECO:0000305}.
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DR EMBL; AE016877; AAP10078.1; -; Genomic_DNA.
DR RefSeq; NP_832877.1; NC_004722.1.
DR PDB; 4RYI; X-ray; 3.49 A; A/B=1-153.
DR PDB; 4RYJ; X-ray; 4.10 A; A/B=1-153.
DR PDB; 4RYM; X-ray; 2.80 A; A=1-153.
DR PDB; 4RYN; X-ray; 2.00 A; A=1-153.
DR PDB; 4RYO; X-ray; 1.60 A; A=1-153.
DR PDB; 4RYQ; X-ray; 1.70 A; A=1-153.
DR PDB; 4RYR; X-ray; 1.70 A; A=1-153.
DR PDBsum; 4RYI; -.
DR PDBsum; 4RYJ; -.
DR PDBsum; 4RYM; -.
DR PDBsum; 4RYN; -.
DR PDBsum; 4RYO; -.
DR PDBsum; 4RYQ; -.
DR PDBsum; 4RYR; -.
DR AlphaFoldDB; Q81BL7; -.
DR SMR; Q81BL7; -.
DR DIP; DIP-61487N; -.
DR STRING; 226900.BC_3136; -.
DR DNASU; 1205483; -.
DR EnsemblBacteria; AAP10078; AAP10078; BC_3136.
DR KEGG; bce:BC3136; -.
DR PATRIC; fig|226900.8.peg.3220; -.
DR HOGENOM; CLU_091805_3_0_9; -.
DR OMA; GLNLIWM; -.
DR Proteomes; UP000001417; 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:0042802; F:identical protein binding; IPI:IntAct.
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 membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..153
FT /note="Tryptophan-rich protein TspO"
FT /id="PRO_0000432574"
FT TRANSMEM 7..27
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:25635100"
FT TRANSMEM 45..65
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:25635100"
FT TRANSMEM 75..95
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:25635100"
FT TRANSMEM 100..120
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:25635100"
FT TRANSMEM 127..149
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:25635100"
FT MUTAGEN 51
FT /note="W->F: Decreases protoporphyrin IX photooxidation.
FT Abolishes protoporphyrin IX photooxidation; when associated
FT with F-138."
FT /evidence="ECO:0000269|PubMed:25635100"
FT MUTAGEN 138
FT /note="W->F: Abolishes protoporphyrin IX photooxidation.
FT Abolishes protoporphyrin IX photooxidation; when associated
FT with F-51."
FT /evidence="ECO:0000269|PubMed:25635100"
FT MUTAGEN 142
FT /note="A->T: Abolishes protoporphyrin IX photooxidation."
FT /evidence="ECO:0000269|PubMed:25635100"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:4RYO"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:4RYO"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:4RYO"
FT HELIX 44..69
FT /evidence="ECO:0007829|PDB:4RYO"
FT HELIX 74..95
FT /evidence="ECO:0007829|PDB:4RYO"
FT HELIX 100..121
FT /evidence="ECO:0007829|PDB:4RYO"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4RYO"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:4RYO"
FT HELIX 133..151
FT /evidence="ECO:0007829|PDB:4RYO"
SQ SEQUENCE 153 AA; 17835 MW; F11E3C2C868285B3 CRC64;
MFMKKSSIIV FFLTYGLFYV SSVLFPIDRT WYDALEKPSW TPPGMTIGMI WAVLFGLIAL
SVAIIYNNYG FKPKTFWFLF LLNYIFNQAF SYFQFSQKNL FLATVDCLLV AITTLLLIMF
SSNLSKVSAW LLIPYFLWSA FATYLSWTIY SIN
