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Database: UniProt
Entry: A0A1G7P3H9_9RHOB
LinkDB: A0A1G7P3H9_9RHOB
Original site: A0A1G7P3H9_9RHOB 
ID   A0A1G7P3H9_9RHOB        Unreviewed;       323 AA.
AC   A0A1G7P3H9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Cytochrome c oxidase subunit 2 {ECO:0000313|EMBL:SDF80845.1};
GN   ORFNames=SAMN04489759_103214 {ECO:0000313|EMBL:SDF80845.1};
OS   Sulfitobacter delicatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=218672 {ECO:0000313|EMBL:SDF80845.1, ECO:0000313|Proteomes:UP000199399};
RN   [1] {ECO:0000313|EMBL:SDF80845.1, ECO:0000313|Proteomes:UP000199399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16477 {ECO:0000313|EMBL:SDF80845.1,
RC   ECO:0000313|Proteomes:UP000199399};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC         [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=7.1.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00029368};
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000256|ARBA:ARBA00007866}.
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DR   EMBL; FNBP01000003; SDF80845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7P3H9; -.
DR   STRING; 218672.SAMN04489759_103214; -.
DR   OrthoDB; 9781261at2; -.
DR   Proteomes; UP000199399; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   CDD; cd04213; CuRO_CcO_Caa3_II; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR   InterPro; IPR045187; CcO_II.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR034236; CuRO_CcO_Caa3_II.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1.
DR   PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS00078; COX2; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS51007; CYTC; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          105..220
FT                   /note="Cytochrome oxidase subunit II copper A binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50857"
FT   DOMAIN          231..323
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   323 AA;  35351 MW;  4CD336F014417AD6 CRC64;
     MRTSALLMGL SLLSACEGRQ SVLNPAGRDA QDVLSLIWVM FGGAVLLWFL LGVIFVYVTK
     VEPREMPRRW GEALIIGGGV IFPVILLGAL LTYSLPMMKP QREADEGLKV HITAEQWWWR
     VAYELPDGRR VTSANELRLP TGRRTGLVLN AHKVIHAFWV PALGGKVDMI PGRETYLSFL
     PEEPGVYRGQ CAEFCGASHA LMAFETVVMT PEDYAEWIEA EASDAAKPAS AEAYRGAEVF
     AREGCGGCHT VRGTQAQGQV GPDLTHVGSR KSLGAGILEM TEDDLSRFIA HTEDIKPEVA
     MPGYDHLTPE DLRALAAYLK GLT
//
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