ID A0A318EG37_9GAMM Unreviewed; 469 AA.
AC A0A318EG37;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
GN ORFNames=C8D93_102503 {ECO:0000313|EMBL:PXV70644.1};
OS Sinimarinibacterium flocculans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Sinimarinibacterium.
OX NCBI_TaxID=985250 {ECO:0000313|EMBL:PXV70644.1, ECO:0000313|Proteomes:UP000248330};
RN [1] {ECO:0000313|EMBL:PXV70644.1, ECO:0000313|Proteomes:UP000248330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 104150 {ECO:0000313|EMBL:PXV70644.1,
RC ECO:0000313|Proteomes:UP000248330};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000256|ARBA:ARBA00007866}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PXV70644.1}.
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DR EMBL; QICN01000002; PXV70644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318EG37; -.
DR OrthoDB; 9773456at2; -.
DR Proteomes; UP000248330; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd13919; CuRO_HCO_II_like_5; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_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; 2.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS51007; CYTC; 2.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
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}; Reference proteome {ECO:0000313|Proteomes:UP000248330};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
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 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 112..254
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT DOMAIN 267..354
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 364..451
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 469 AA; 51696 MW; 8AA0A4C63F40A5C1 CRC64;
MAIAIALILL LAGSILFHFL SPWQLTPLAS NWGSIDDTIG ITFWVTGFVF VAVNVFMAWA
IVRYRWRADR RAEYEPENKK LEWWLIGVTT VGIAALLAPG LFVWASYVTV PDDAHEVEVV
GQQWHWGFRF PGEDGSFGRV DTRLVTGDNP FGMDASDPAG HDDVLVHGSR VRLPVDRPVK
ALLRSRDVLH NFQVAQFRAK MDLVPGQLSY LWVTPTRTGE FEILCAELCG IGHFAMRGMV
EVVEPEVFEQ WLAAQPTYAS ELARAAPDAA AGKALYTPCA ACHGAEGQGN VQMNAPRLAG
QDAWYLIRQL EYFKAGARGA HPDDTHGQQM RAFAGMLADR AAMADLAAYV ETFPEPPPVI
SIDGNPQRGA RVWRNCGACH GSEGQGLQAT QAPRLAGQDD WYLERQLENF RRGIRGRHPG
DAYGWQMAEM AKLLRDDDAT RDLIAHINTL ALAAAPAPAD PTALARRTD
//
