ID A0A0M2VDH7_9GAMM Unreviewed; 465 AA.
AC A0A0M2VDH7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Cytochrome D ubiquinol oxidase subunit I {ECO:0000313|EMBL:KKO48997.1};
GN ORFNames=VT06_08380 {ECO:0000313|EMBL:KKO48997.1};
OS Arsukibacterium sp. MJ3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Arsukibacterium.
OX NCBI_TaxID=1632859 {ECO:0000313|EMBL:KKO48997.1, ECO:0000313|Proteomes:UP000034895};
RN [1] {ECO:0000313|EMBL:KKO48997.1, ECO:0000313|Proteomes:UP000034895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:KKO48997.1,
RC ECO:0000313|Proteomes:UP000034895};
RA Lylloff J.E., Skov L.B., Jepsen M., Hallin P.F., Sorensen S.J.,
RA Stougaard P., Glaring M.A.;
RT "Draft genome sequences of two protease-producing strains of
RT Arsukibacterium isolated from two cold and alkaline environments.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|PIRNR:PIRNR006446}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 1
CC family. {ECO:0000256|ARBA:ARBA00009819, ECO:0000256|PIRNR:PIRNR006446}.
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:KKO48997.1}.
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DR EMBL; LAHP01000009; KKO48997.1; -; Genomic_DNA.
DR RefSeq; WP_046553848.1; NZ_LAHP01000009.1.
DR AlphaFoldDB; A0A0M2VDH7; -.
DR STRING; 1632859.VT06_08380; -.
DR PATRIC; fig|1632859.4.peg.1740; -.
DR OrthoDB; 9807042at2; -.
DR Proteomes; UP000034895; Unassembled WGS sequence.
DR GO; GO:0070069; C:cytochrome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR InterPro; IPR002585; Cyt-d_ubiquinol_oxidase_su_1.
DR PANTHER; PTHR30365:SF14; CYTOCHROME BD2 SUBUNIT I; 1.
DR PANTHER; PTHR30365; CYTOCHROME D UBIQUINOL OXIDASE; 1.
DR Pfam; PF01654; Cyt_bd_oxida_I; 1.
DR PIRSF; PIRSF006446; Cyt_quinol_oxidase_1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR006446};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR006446};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006446};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Reference proteome {ECO:0000313|Proteomes:UP000034895};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006446}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 55..76
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 96..118
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 125..146
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 183..206
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 218..236
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 318..343
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 404..428
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT REGION 439..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 51821 MW; 5958454536C3C70A CRC64;
MELDPLLLSR VQFAFVVCFH AIFPVFTIGL ASFIAVLEAL SFKTGNPLWQ KLSKFWLQVF
AVVFGMGVVS GIVMSFQFGT NWSNFSYATA NFLGPVLSYE VITAFFLEAA FLGVLLFGRD
KVPQGVHLFA AIMVALGTFI SSFWILSANS LMHTPDGLEL RNGMYHVVSW ADALFTESFA
YRFAHMALAS FLTAALVVAG VSAWFILQNR EFDTNRKALS IALWMLLILA PLQVVVGDFH
GLNTLKHQPM KVAAMEGNWE TGTGVPLLLF AIPDQEAQTN HFEVKIPKLA SYVLTHDWNG
EVPGLNEVTP DKQPPVFIVF WAFRIMVAMG LLMVLFALWG LVLRYKGRYY QSNRFLQGLR
LMSLSPFIAV LTGWVVTEAG RAPWLIYNQM THAEGLTPSL TGGMALFTLI GYIVVYALVF
SSGVYYLLKV FRGGVEKANR PHEQEEVERP KRPFSAAHAS LEGDQ
//
