ID I7GYH7_9HELI Unreviewed; 522 AA.
AC I7GYH7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Cytochrome bd quinol oxidase subunit I {ECO:0000313|EMBL:BAM31316.1};
DE EC=1.10.3.- {ECO:0000313|EMBL:BAM31316.1};
GN Name=cydA {ECO:0000313|EMBL:BAM31316.1};
GN ORFNames=HCBAA847_0056 {ECO:0000313|EMBL:BAM31316.1};
OS Helicobacter cinaedi CCUG 18818 = ATCC BAA-847.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537971 {ECO:0000313|EMBL:BAM31316.1, ECO:0000313|Proteomes:UP000006036};
RN [1] {ECO:0000313|EMBL:BAM31316.1, ECO:0000313|Proteomes:UP000006036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM31316.1,
RC ECO:0000313|Proteomes:UP000006036};
RX PubMed=23012276; DOI=10.1128/JB.01347-12;
RA Miyoshi-Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RT "Complete Genome Sequence of Helicobacter cinaedi Type Strain ATCC
RT BAA-847.";
RL J. Bacteriol. 194:5692-5692(2012).
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}.
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DR EMBL; AP012492; BAM31316.1; -; Genomic_DNA.
DR AlphaFoldDB; I7GYH7; -.
DR KEGG; hcb:HCBAA847_0056; -.
DR PATRIC; fig|1206745.3.peg.59; -.
DR eggNOG; COG1271; Bacteria.
DR HOGENOM; CLU_030555_3_1_7; -.
DR OrthoDB; 9807042at2; -.
DR Proteomes; UP000006036; Chromosome 1.
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; 2.
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:BAM31316.1};
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 20..46
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 58..77
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 97..123
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 189..213
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 225..243
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 395..417
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 429..451
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 480..501
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
SQ SEQUENCE 522 AA; 57964 MW; F3E5640876096AF9 CRC64;
MDMVNELASV DWARAQFALT ALYHFLFVPL TLGLSFIVAI METIYVKTDN PQWRKITRFW
LTLFAINFAI GVATGIIMEF EFGTNWANYS WFVGDIFGAP LAVEGIMAFF LEATFFAVMF
FGWDKVSKKF HLLSTWFVAI GSNLSAFWIL VANGWMQYPI GTIFNPDTAR NEMSSFAEVA
LSPVAVSKFL HTVASGYVIS ALFVMGISAL YLLRGRFISE AKKSLIVGAS FGLITSMFLF
FSGDESAYRV TQHQPMKLAA MEGIYQGEHR AGITAFGILN PDKKPGDEKE VFLFDITIPY
ALSILGNRSP NSFVPGIEDL LHGNEKQGIT GIDSRIQSGK LALSALKDYK EAKAQNDTEA
MNFNRGILES NMPNFGYGYL EKPEDAIPPI ALTFYSFHIM VALGSAFFVL FIVVLYLAMA
NNVVQFRKIL WLCVIAIPFG YIAAEAGWII AEVGRQPWAI QDLLPVGIAA THLSSVHIQV
SFFIFAFLFT TLLCAEIGIM IKSIKKGFVE EHSVDSTHKG GK
//