ID A1UHI2_MYCSK Unreviewed; 347 AA.
AC A1UHI2;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Cytochrome bd quinol oxidase subunit 2 apoprotein {ECO:0000313|EMBL:ABL92290.1};
DE EC=1.10.3.- {ECO:0000313|EMBL:ABL92290.1};
DE Flags: Precursor;
GN OrderedLocusNames=Mkms_3096 {ECO:0000313|EMBL:ABL92290.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL92290.1};
RN [1] {ECO:0000313|EMBL:ABL92290.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL92290.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) 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 ubiquinol oxidase subunit 2
CC family. {ECO:0000256|ARBA:ARBA00007543}.
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DR EMBL; CP000518; ABL92290.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UHI2; -.
DR STRING; 189918.Mkms_3096; -.
DR KEGG; mkm:Mkms_3096; -.
DR HOGENOM; CLU_049294_0_1_11; -.
DR OrthoDB; 9776710at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR003317; Cyt-d_oxidase_su2.
DR NCBIfam; TIGR00203; cydB; 1.
DR PANTHER; PTHR43141:SF5; CYTOCHROME BD-I UBIQUINOL OXIDASE SUBUNIT 2; 1.
DR PANTHER; PTHR43141; CYTOCHROME BD2 SUBUNIT II; 1.
DR Pfam; PF02322; Cyt_bd_oxida_II; 1.
DR PIRSF; PIRSF000267; Cyt_oxidse_sub2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:ABL92290.1};
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 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 347 AA; 37896 MW; 94BF9C974B23BAC7 CRC64;
MGLQELWFIL IAALFLGFLV LEGFDFGVGM LMAPMGIVGE GTPETRRRAV LNTIGPVWDA
NEVWLITAGA SMFAAFPVWY ATVFSALYLP LLAILFGMIL RIVGIEWRGK IDDPTWRRRA
DWGIALGSWL PAILWGVAFA VLVRGLPVDA EQQVVGLTFG DVVNAYTLLG GLATCSLFLF
YGSTFLALKT SGPVRDDAFR FVRILSAPVI VLAGGFGLWT QLAYGKPWTW AALAAAVVAL
LVAVALMWTG GREGWAFVST VVVVAAVATL IFGTLYPYLL NSTLNPEWGV TIFNGSSTPY
TLKIMSWASL TLLPLVLIYQ GWTYWVFRQR ISADRIPESV GLSKQAP
//
