ID L7UKD0_MYXSD Unreviewed; 348 AA.
AC L7UKD0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
GN OrderedLocusNames=MYSTI_06704 {ECO:0000313|EMBL:AGC47977.1};
OS Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC47977.1, ECO:0000313|Proteomes:UP000011131};
RN [1] {ECO:0000313|EMBL:AGC47977.1, ECO:0000313|Proteomes:UP000011131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC {ECO:0000313|Proteomes:UP000011131};
RX PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT fruiting myxobacterium.";
RL Genome Announc. 1:E0010013-E0010013(2013).
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}.
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DR EMBL; CP004025; AGC47977.1; -; Genomic_DNA.
DR RefSeq; WP_015352231.1; NC_020126.1.
DR AlphaFoldDB; L7UKD0; -.
DR STRING; 1278073.MYSTI_06704; -.
DR KEGG; msd:MYSTI_06704; -.
DR PATRIC; fig|1278073.3.peg.6807; -.
DR eggNOG; COG1622; Bacteria.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_036876_1_0_7; -.
DR OMA; FRIKMDA; -.
DR OrthoDB; 9781261at2; -.
DR Proteomes; UP000011131; Chromosome.
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; cd13915; CuRO_HCO_II_like_2; 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; 1.
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; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR NCBIfam; TIGR02866; CoxB; 1.
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 SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS51007; CYTC; 1.
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}; Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
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 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 100..211
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT DOMAIN 235..330
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 348 AA; 39395 MW; 6287714EE62A4C74 CRC64;
MSELLNNLLF LPESASTFAE RVDLLHHFVV ITTIVMSTGT GLAALFMFFR YRRRTPAQAT
EYVVPTLKTE FLFVSVPLVF FLAWFGIGFR DFTWVTTPPK DSMDVYVMGK QWMWKFSYPE
GPNGVNVLHV PANRPVRLLI TSRDVLHSFY VPSFRIKMDA LPGRYTQIWF EATKPGTYQV
LCTEYCGLSH SKMLAEVVVL PQEEYDNWIK EQRRGRLQDR QDALADTSLV PPVARMVEQG
QVLAGTQGCL KCHSVDGSQH IGPTFLGMYD RMEKLDDGQQ IRVDEAYITQ SMMDPGAHLV
SGYQNVMPTY QGKLQGPETA AIVEYIKSLR TPAVREGASE GPAYDPIQ
//