ID   CP141_MYCTO             Reviewed;         400 AA.
AC   P9WPL6; L0TBL6; O08362;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Putative cytochrome P450 141;
DE            EC=1.14.-.-;
GN   Name=cyp141; OrderedLocusNames=MT3203;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47543.1; -; Genomic_DNA.
DR   PIR; H70921; H70921.
DR   RefSeq; WP_003899925.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPL6; -.
DR   SMR; P9WPL6; -.
DR   EnsemblBacteria; AAK47543; AAK47543; MT3203.
DR   KEGG; mtc:MT3203; -.
DR   PATRIC; fig|83331.31.peg.3453; -.
DR   HOGENOM; CLU_033716_1_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..400
FT                   /note="Putative cytochrome P450 141"
FT                   /id="PRO_0000426930"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         346
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  43732 MW;  C612759A4F1B85B5 CRC64;
     MTSTSIPTFP FDRPVPTEPS PMLSELRNSC PVAPIELPSG HTAWLVTRFD DVKGVLSDKR
     FSCRAAAHPS SPPFVPFVQL CPSLLSIDGP QHTAARRLLA QGLNPGFIAR MRPVVQQIVD
     NALDDLAAAE PPVDFQEIVS VPIGEQLMAK LLGVEPETVH ELAAHVDAAM SVCEIGDEEV
     SRRWSALCTM VIDILHRKLA EPGDDLLSTI AQANRQQSTM TDEQVVGMLL TVVIGGVDTP
     IAVITNGLAS LLHHRDQYER LVEDPGRVAR AVEEIVRFNP ATEIEHLRVV TEDVVIAGTA
     LSAGSPAFTS ITSANRDSDQ FLDPDEFDVE RNPNEHIAFG YGPHACPASA YSRMCLTTFF
     TSLTQRFPQL QLARPFEDLE RRGKGLHSVG IKELLVTWPT