ID T1CMM3_9HELI Unreviewed; 533 AA.
AC T1CMM3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Cytochrome d ubiquinol oxidase subunit I {ECO:0000313|EMBL:GAD18009.1};
DE EC=1.10.3.- {ECO:0000313|EMBL:GAD18009.1};
GN ORFNames=HFN_1568 {ECO:0000313|EMBL:GAD18009.1};
OS Helicobacter fennelliae MRY12-0050.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1325130 {ECO:0000313|EMBL:GAD18009.1, ECO:0000313|Proteomes:UP000018143};
RN [1] {ECO:0000313|EMBL:GAD18009.1, ECO:0000313|Proteomes:UP000018143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRY12-0050 {ECO:0000313|EMBL:GAD18009.1,
RC ECO:0000313|Proteomes:UP000018143};
RA Rimbara E., Matsui M., Mori S., Suzuki S., Suzuki M., Kim H., Sekizuka T.,
RA Kuroda M., Shibayama K.;
RT "Draft Genome Sequence of Helicobacter fennelliae Strain MRY12-0050,
RT Isolated from a Bacteremia Patient.";
RL Genome Announc. 1:e00512-13(2013).
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 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:GAD18009.1}.
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DR EMBL; BASD01000003; GAD18009.1; -; Genomic_DNA.
DR RefSeq; WP_023946249.1; NZ_BASD01000003.1.
DR AlphaFoldDB; T1CMM3; -.
DR STRING; 1325130.HFN_1568; -.
DR eggNOG; COG1271; Bacteria.
DR OrthoDB; 9807042at2; -.
DR Proteomes; UP000018143; Unassembled WGS sequence.
DR GO; GO:0070069; C:cytochrome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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:SF0; CYTOCHROME BD-I UBIQUINOL OXIDASE SUBUNIT 1; 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 Oxidoreductase {ECO:0000313|EMBL:GAD18009.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018143};
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 16..41
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 53..72
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 92..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 184..208
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 392..414
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 426..448
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 477..498
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
SQ SEQUENCE 533 AA; 59418 MW; 70467A44F2A72840 CRC64;
MDLHVDWSRA QFGLTAIYHF LFVPLTLGLS FIVAIMESIY VKTNNPQWRT ITKFWLTLFA
INFAIGVATG LIMEFEFGTN WANYSWFVGD IFGAPLAIEG IFAFFLEATF FAVMFFGWDR
VSKKFHLLST WLVAIGSNLS AFWILVANGW MQYPVGTIFN PNTARNEMAD ILEVIFSPVA
ISKFLHTIAS GYVIASLFVM GISAWFLLKN KESKEVLMAK KSLVVGASFG LLTSMFLFFS
GDESAYQVTQ KQPLKLAAME GIYDGEHRAG LIAFGILNPA KKPGDSEPTF LFDITIPYAL
SILGQRDTQG FIPGINDLIY GNKEKNIESV SERMLRGQIA LKALSQYQEL KKQNGVENEE
LAQIVQENMK DFGYGYLKAP EDAVPPVALT FYSFHIMVAL GSAFFVLFII ALYLAMTNDI
ARFRKVLWLC VIAIPFGYVA AEAGWIVAEV GRQPWAIQNL LPVHIAATNL SHTNIQISFF
LFLALFSTLL LAEVGIMIRA IKKGFGAHVG HLVDSVDSID FTTRAESNTK SAR
//
