COXX2_BACSU
ID COXX2_BACSU Reviewed; 305 AA.
AC P24009;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protoheme IX farnesyltransferase 2;
DE EC=2.5.1.141 {ECO:0000269|PubMed:19204012};
DE AltName: Full=Heme B farnesyltransferase 2;
DE AltName: Full=Heme O synthase 2;
GN Name=ctaB2; OrderedLocusNames=BSU14880;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1847686; DOI=10.1111/j.1432-1033.1991.tb15732.x;
RA Saraste M., Metso T., Nakari T., Jalli T., Lauraeus M., van der Oost J.;
RT "The Bacillus subtilis cytochrome-c oxidase. Variations on a conserved
RT protein theme.";
RL Eur. J. Biochem. 195:517-525(1991).
RN [2]
RP SEQUENCE REVISION TO 46-47 AND 221.
RA Hederstedt L.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Bertero M., Presecan E., Glaser P., Richou A., Danchin A.;
RT "Bacillus subtilis chromosomal region downstream nprE.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5]
RP INTERACTION WITH CTAA.
RX PubMed=15491161; DOI=10.1021/bi048469k;
RA Brown B.M., Wang Z., Brown K.R., Cricco J.A., Hegg E.L.;
RT "Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter
RT sphaeroides interact in Escherichia coli.";
RL Biochemistry 43:13541-13548(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-199.
RX PubMed=19204012; DOI=10.1093/jb/mvp024;
RA Mogi T.;
RT "Over-expression and characterization of Bacillus subtilis heme O
RT synthase.";
RL J. Biochem. 145:669-675(2009).
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:0000269|PubMed:19204012}.
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;
CC Evidence={ECO:0000269|PubMed:19204012};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme O biosynthesis;
CC heme O from protoheme: step 1/1.
CC -!- SUBUNIT: Interacts with CtaA. {ECO:0000269|PubMed:15491161}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined
CC according to the Fischer nomenclature.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. Protoheme IX
CC farnesyltransferase subfamily. {ECO:0000305}.
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DR EMBL; X54140; CAA38075.1; -; Genomic_DNA.
DR EMBL; Z98682; CAB11341.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13361.1; -; Genomic_DNA.
DR PIR; C69609; C69609.
DR RefSeq; NP_389371.1; NC_000964.3.
DR RefSeq; WP_003232250.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P24009; -.
DR SMR; P24009; -.
DR IntAct; P24009; 9.
DR STRING; 224308.BSU14880; -.
DR PaxDb; P24009; -.
DR PRIDE; P24009; -.
DR EnsemblBacteria; CAB13361; CAB13361; BSU_14880.
DR GeneID; 935922; -.
DR KEGG; bsu:BSU14880; -.
DR PATRIC; fig|224308.179.peg.1622; -.
DR eggNOG; COG0109; Bacteria.
DR InParanoid; P24009; -.
DR OMA; QFFWQFP; -.
DR PhylomeDB; P24009; -.
DR BioCyc; BSUB:BSU14880-MON; -.
DR BioCyc; MetaCyc:BSU14880-MON; -.
DR BRENDA; 2.5.1.141; 658.
DR UniPathway; UPA00834; UER00712.
DR Proteomes; UP000001570; 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:0004311; F:farnesyltranstransferase activity; IBA:GO_Central.
DR GO; GO:0008495; F:protoheme IX farnesyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR43448; PTHR43448; 1.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Heme biosynthesis; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..305
FT /note="Protoheme IX farnesyltransferase 2"
FT /id="PRO_0000162905"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 199
FT /note="H->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:19204012"
SQ SEQUENCE 305 AA; 33946 MW; 77204E64E79C59A1 CRC64;
MANSRILNDT AIDGQIEETT AWKDFLSLIK IGIVNSNLIT TFTGMWLALH ISGLSFLGNI
NTVLLTLIGS SLIIAGSCAI NNWYDRDIDH LMERTKVRPT VTGKIQPSQA LWSGILLVAL
GLIMLLMTTV MAAVIGFIGV FTYVVLYTMW TKRRYTINTV VGSVSGAVPP LIGWTAVEGN
IGVVAWVLFM ILFIWQIPHF LALAIKKTED YRAANIPMLP VVYGFEVTKR QIIVWVACLM
PLPFFLGSLG LPIVILGLLL NIGWLILGLM GFRSKNIMKW ATQMFVYSLN YMTIYFVAMV
VLTLF
