ID   COXX_STAHJ              Reviewed;         303 AA.
AC   Q4L5D0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Protoheme IX farnesyltransferase {ECO:0000255|HAMAP-Rule:MF_00154};
DE            EC=2.5.1.141 {ECO:0000255|HAMAP-Rule:MF_00154};
DE   AltName: Full=Heme B farnesyltransferase {ECO:0000255|HAMAP-Rule:MF_00154};
DE   AltName: Full=Heme O synthase {ECO:0000255|HAMAP-Rule:MF_00154};
GN   Name=ctaB {ECO:0000255|HAMAP-Rule:MF_00154}; OrderedLocusNames=SH1836;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Converts heme B (protoheme IX) to heme O by substitution of
CC       the vinyl group on carbon 2 of heme B porphyrin ring with a
CC       hydroxyethyl farnesyl side group. {ECO:0000255|HAMAP-Rule:MF_00154}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate +
CC         Fe(II)-heme o; Xref=Rhea:RHEA:28070, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:60344, ChEBI:CHEBI:60530,
CC         ChEBI:CHEBI:175763; EC=2.5.1.141; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00154};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; heme O biosynthesis;
CC       heme O from protoheme: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00154}.
CC   -!- SUBUNIT: Interacts with CtaA. {ECO:0000255|HAMAP-Rule:MF_00154}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00154};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00154}.
CC   -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC       according to the Fischer nomenclature. {ECO:0000255|HAMAP-
CC       Rule:MF_00154}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. Protoheme IX
CC       farnesyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_00154}.
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DR   EMBL; AP006716; BAE05145.1; -; Genomic_DNA.
DR   RefSeq; WP_011276112.1; NC_007168.1.
DR   AlphaFoldDB; Q4L5D0; -.
DR   SMR; Q4L5D0; -.
DR   STRING; 279808.SH1836; -.
DR   EnsemblBacteria; BAE05145; BAE05145; SH1836.
DR   GeneID; 58062041; -.
DR   KEGG; sha:SH1836; -.
DR   eggNOG; COG0109; Bacteria.
DR   HOGENOM; CLU_029631_0_0_9; -.
DR   OMA; QFFWQFP; -.
DR   OrthoDB; 1875497at2; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000000543; 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:0008495; F:protoheme IX farnesyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048034; P:heme O biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd13957; PT_UbiA_Cox10; 1.
DR   Gene3D; 1.10.357.140; -; 1.
DR   HAMAP; MF_00154; CyoE_CtaB; 1.
DR   InterPro; IPR006369; Protohaem_IX_farnesylTrfase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR044878; UbiA_sf.
DR   PANTHER; PTHR43448; PTHR43448; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Heme biosynthesis; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..303
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000327166"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        175..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ   SEQUENCE   303 AA;  33730 MW;  18B44FCA65264041 CRC64;
     MSKEQTLSQP SSRVSFKELQ QIIKMGLVQG NLIPAFAGAW LAVVMSNHSF LSSIPQILLM
     LIGSTLIMGG ACALNNYYDQ DIDRIMPSKQ NRPTVNDRIS DKNLLILSFG MMLLGEACLF
     LLNVPSGVLG LIGIVGYVSY YSIWSKRHTT WNTVVGSFPG AVPPLIGWVA IDGNISLIAI
     ALFLVVFCWQ PIHFYALAIK RSDEYSLANI PMLPSVKGFK RTRISMFIWL VFLLPLPFLL
     SSLGTTFVVL ATLLNLGWLY VGLTSFKKAT DQTKWATKMF IYSLNYLVVF FVLVVVISLI
     KMI