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Database: UniProt
Entry: E1AA77_NEIME
LinkDB: E1AA77_NEIME
Original site: E1AA77_NEIME 
ID   E1AA77_NEIME            Unreviewed;       365 AA.
AC   E1AA77;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Cytochrome c oxidase subunit III {ECO:0000256|ARBA:ARBA00029635};
GN   Name=ccoP {ECO:0000313|EMBL:ADM88992.1};
OS   Neisseria meningitidis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=487 {ECO:0000313|EMBL:ADM88992.1};
RN   [1] {ECO:0000313|EMBL:ADM88992.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OX9930134 {ECO:0000313|EMBL:ADM88992.1}, OX9930254
RC   {ECO:0000313|EMBL:ADM88993.1}, and OX9930310
RC   {ECO:0000313|EMBL:ADM88994.1};
RX   PubMed=20808844; DOI=10.1371/journal.ppat.1001055;
RA   Aspholm M., Aas F.E., Harrison O.B., Quinn D., Vik A., Viburiene R.,
RA   Tonjum T., Moir J., Maiden M.C., Koomey M.;
RT   "Structural alterations in a component of cytochrome c oxidase and
RT   molecular evolution of pathogenic Neisseria in humans.";
RL   PLoS Pathog. 6:e1001055-e1001055(2010).
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000256|ARBA:ARBA00001926};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00004673}.
CC   -!- SIMILARITY: Belongs to the CcoP / FixP family.
CC       {ECO:0000256|ARBA:ARBA00006113}.
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DR   EMBL; HM543252; ADM88992.1; -; Genomic_DNA.
DR   EMBL; HM543253; ADM88993.1; -; Genomic_DNA.
DR   EMBL; HM543254; ADM88994.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1AA77; -.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:1902600; P:proton transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.280.130; -; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   InterPro; IPR032858; CcoP_N.
DR   InterPro; IPR038414; CcoP_N_sf.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR008168; Cyt_C_IC.
DR   InterPro; IPR004678; Cyt_c_oxidase_cbb3_su3.
DR   NCBIfam; TIGR00782; ccoP; 1.
DR   PANTHER; PTHR33751; CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP; 1.
DR   PANTHER; PTHR33751:SF1; CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 2.
DR   Pfam; PF14715; FixP_N; 1.
DR   PRINTS; PR00605; CYTCHROMECIC.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          134..213
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          222..305
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          308..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   365 AA;  40039 MW;  EFCC2552A51EB4B4 CRC64;
     MNTTSQFTSN FWNIYIAVIV LLSFIALAWL LLSQNVVKRP KKGEEVQTTG HEWDGIAEYD
     NPLPRWWFWL CVLTWLFGIG YLVMYPGVGD YKGLLKWTSH NQYEKEVKKA DEQYGKLYAK
     FADMPIEKVA KDPQAKQIAQ NLFNTYCIQC HGSDAKGSKG FPNLTDSDWL WGGDPDKIHE
     TIEKGRVATM PAWGPALGEE GVKDVAHYVM SLSKPEGQYD EERAARGQAL FSGPPANCFT
     CHGDKGQGIQ GLGPNLTDDV WLWGGTQKSI IETITNGRSS QMPAWGHFLD KDKLHIMTAY
     VWGLSDKDGK APVKKAEPAP TPAPAAEPAA SAPVEAAQAA SEAKPAAAEP KAEEKAAPAA
     KADGK
//
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