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Database: UniProt
Entry: A0A212S586_RHOAC
LinkDB: A0A212S586_RHOAC
Original site: A0A212S586_RHOAC 
ID   A0A212S586_RHOAC        Unreviewed;       386 AA.
AC   A0A212S586;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Cytochrome bd-I ubiquinol oxidase subunit 2 apoprotein {ECO:0000313|EMBL:SNB80370.1};
GN   ORFNames=SAMN06265338_1137 {ECO:0000313|EMBL:SNB80370.1};
OS   Rhodoblastus acidophilus (Rhodopseudomonas acidophila).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Rhodoblastus.
OX   NCBI_TaxID=1074 {ECO:0000313|EMBL:SNB80370.1, ECO:0000313|Proteomes:UP000198418};
RN   [1] {ECO:0000313|Proteomes:UP000198418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 137 {ECO:0000313|Proteomes:UP000198418};
RA   Varghese N., Submissions S.;
RL   Submitted (JUN-2017) 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; FYDG01000013; SNB80370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212S586; -.
DR   OrthoDB; 9776710at2; -.
DR   Proteomes; UP000198418; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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   Reference proteome {ECO:0000313|Proteomes:UP000198418};
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        12..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        210..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        299..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        342..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   386 AA;  41575 MW;  0CB5FBE30153D5F5 CRC64;
     MFDFLDYATL KFIWWILVGA LLMGFAIADG MDMGVGVLLP FVARADAERR IAINTVGPHW
     DGNQVWLITA GGAIFAAWPA VYAAAFSGFY MAMLLVLFAL FFRPVGFDYR SKIDNDVWRS
     AWDWGLFVGG AVPALIFGVA FGNLLQGVPF HLDDMLRPHY QGSLLTALLP LLNPFARLAG
     AISLGMFTVH GGLWLQLRAD DPVASRARKT VMALAPAVAL LFLGAGVWLW FGVDGYRVIS
     APAHDALPNP LAKEVVRATH AWFDIYAAVP AAAAAPVAGV LGPLVAATLA FARRPGWGFV
     ASALGMVGVI GSAGLSMFPF IMPSSLDPRS SLTIWDAPSS HLTLTVMLIA TAIFLPIVLG
     YTIWCYANMW GRVTAKEIEA QSHSAY
//
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