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Database: UniProt
Entry: A0A1T2L8L8_9GAMM
LinkDB: A0A1T2L8L8_9GAMM
Original site: A0A1T2L8L8_9GAMM 
ID   A0A1T2L8L8_9GAMM        Unreviewed;       486 AA.
AC   A0A1T2L8L8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE            EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
GN   ORFNames=BOW52_04615 {ECO:0000313|EMBL:OOZ41431.1};
OS   Solemya elarraichensis gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1918949 {ECO:0000313|EMBL:OOZ41431.1, ECO:0000313|Proteomes:UP000190198};
RN   [1] {ECO:0000313|EMBL:OOZ41431.1, ECO:0000313|Proteomes:UP000190198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sp-SM6 {ECO:0000313|EMBL:OOZ41431.1};
RA   Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT   "Mixed transmission modes and dynamic genome evolution in an obligate
RT   animal-bacterial symbiosis.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604677-50};
CC       Note=Binds 1 copper ion per subunit, denoted as copper B.
CC       {ECO:0000256|PIRSR:PIRSR604677-50};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604677-50};
CC       Note=Binds 2 heme groups per subunit, denoted as high- and low-spin.
CC       {ECO:0000256|PIRSR:PIRSR604677-50};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00004673}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000256|ARBA:ARBA00009578, ECO:0000256|RuleBase:RU000370}.
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:OOZ41431.1}.
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DR   EMBL; MPRK01000062; OOZ41431.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T2L8L8; -.
DR   OrthoDB; 9806838at2; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000190198; Unassembled WGS sequence.
DR   GO; GO:0045278; C:plasma membrane respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1.
DR   InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR004677; Cyt_c_oxidase_cbb3_su1.
DR   NCBIfam; TIGR00780; ccoN; 1.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF29; CYTOCHROME C OXIDASE SUBUNIT 1 HOMOLOG, BACTEROID; 1.
DR   Pfam; PF00115; COX1; 1.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Electron transport {ECO:0000256|RuleBase:RU000370};
KW   Heme {ECO:0000256|PIRSR:PIRSR604677-50, ECO:0000256|RuleBase:RU000370};
KW   Iron {ECO:0000256|PIRSR:PIRSR604677-50};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604677-50};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000370};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000370};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000370}.
FT   TRANSMEM        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        208..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        347..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        389..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        433..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..486
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
FT   BINDING         63
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1; low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         212
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         262
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         263
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         350
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="2; high-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         352
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1; low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
SQ   SEQUENCE   486 AA;  54819 MW;  9313DCFFCE809C03 CRC64;
     MAHEAAAADS QYNYDIIKRF AVMALVWGIL GMFAGTYIAA ELAFPFLNFD TPQITFGRLR
     PVHTTLVIFG FGGSALFATS YYVVQRTCQT PLSSNMLAGF TFWGWQASVL LGVLGYVNGY
     TQGREYAEFV WPIDLLITVT WVAYFYVYVT TLMRRSQPHI YVANWFYMSF ILATAILHIV
     NNLAVPVSMF SLQSYSAFAG VQDAMTQWWY GHNAVGFFLT AAFLGMMYYF VPKQAGRPVY
     SYRLSIVHFW ALAFLYMWVG AHHLHWTALP DWTSSLAATF SILLLMPSWG GMINGIMTLS
     GAWDKLRTDP IMLFLITSLA FYGMSTFEGP MMSLKSVNAL SHYTDWTIGH VHSGALGWVA
     MISFGSFYHM IPRLWDTRLW SKKLVYTHFW LATIGIVLYI TAMWISGIGQ GLMLRAFDDY
     GNLAYTFIES VSFMHVPLVT RMLGGIFFVA GILIMAFNVF MTVRTAKREQ AEIEAKIAAK
     MAKAGA
//
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