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3.D.4.4.1
Cytochrome oxidase including heme A synthase (HAS) and 4 subunits of the cytochrome oxidase.  The 3-d structure of heme A synthase (of 306 aas and 8 TMSs) at 2.2 Å resolution has been solved revealing that the N- and C-terminal halves of HAS consist of four-helix bundles and they align in a pseudo twofold symmetry manner. Each bundle contains a pair of histidine residues and forms a heme-binding domain. The C-half domain binds a cofactor-heme molecule, while the N-half domain is vacant (Niwa et al. 2018). The Sco1 protein, YpmQ, is an accessory protein involved in the assembly of cytochrome c oxidase (Andrews et al. 2004).

Accession Number:P24012
Protein Name:Cytochrome c oxidase subunit 3
Length:207
Molecular Weight:23266.00
Species:Bacillus subtilis [1423]
Number of TMSs:5
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate hydron

Cross database links:

Entrez Gene ID: 935993   
Pfam: PF00510   
KEGG: bsu:BSU14910   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0004129 F:cytochrome-c oxidase activity
GO:0019646 P:aerobic electron transport chain

References (2)

[1] “The Bacillus subtilis cytochrome-c oxidase. Variations on a conserved protein theme.”  Saraste M.et.al.   1847686
[2] “The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.”  Kunst F.et.al.   9384377

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MQVQEKFTAE TFPASPEKVT LEGKNKFLGF WLFLGGETVL FASLFATFLA LRNSNAGDPP 
61:	TTEMFDVTLV FIATMLLLTS SLTSVYAMYH MKNFSFGKMQ LWLGITILLG AGFLGLEIYE 
121:	FKHYTHEFGF TITSSALGSA FYTLVGTHGA HVAFGLMWIS TLMIRNAKRG LNLYTAPKFY 
181:	VASLYWHFID VVWVFIFTVV YLMGMVG