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Database: UniProt
Entry: A4G4V9_HERAR
LinkDB: A4G4V9_HERAR
Original site: A4G4V9_HERAR 
ID   A4G4V9_HERAR            Unreviewed;       533 AA.
AC   A4G4V9;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Cytochrome d ubiquinol oxidase subunit 1 (Cytochrome d ubiquinol oxidase subunit I) (Cytochrome bd-I oxidase subunit I) {ECO:0000313|EMBL:CAL61546.1};
DE            EC=1.10.3.- {ECO:0000313|EMBL:CAL61546.1};
GN   Name=cydA {ECO:0000313|EMBL:CAL61546.1};
GN   OrderedLocusNames=HEAR1374 {ECO:0000313|EMBL:CAL61546.1};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL61546.1, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL61546.1, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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}.
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DR   EMBL; CU207211; CAL61546.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4G4V9; -.
DR   STRING; 204773.HEAR1374; -.
DR   KEGG; har:HEAR1374; -.
DR   eggNOG; COG1271; Bacteria.
DR   HOGENOM; CLU_030555_0_1_4; -.
DR   OrthoDB; 9807042at2; -.
DR   Proteomes; UP000006697; Chromosome.
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: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:CAL61546.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006697};
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..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        55..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        93..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        129..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        185..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        221..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        393..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        427..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        469..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   REGION          509..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   533 AA;  58537 MW;  D36CAA2D0C240EF1 CRC64;
     MELDIVSLSR LQFAITALYH FLFVPLTIGL AILLAIMETV YVMTDRVIWR DMTKFWGALF
     GINFAMGVAT GVVMEFQFGM NWSYYSHYVG DIFGAPLAIE GLMAFFLEAT FVGLFFFGWD
     KLSKVGHLIT TWAVAIGSNF SALWILIANG WMQNPVGAAL NPETMRMEVT DFAAVLTNPV
     AQAKFVHTVS AGYVTAAIFV LGVSAWYVLK GRHLELAKRS MTVAASFGLA AALSVVVLGD
     ESGYLSTEHQ KMKLAAIEGM WETQPAPASF TLIGFPNQEA RETHYAIHIP WVMGLIGTRS
     LDTVIPGINE LVQHAELRIA NGIQAYDALQ KIRAVGQGEK ITPAMRFAFE ETGGDLGYAL
     LLKRYVDDPR QATPAQITQA ALDTVPQVAP LFWLFRIMVG IGMFLILLTG TFFFLSARRQ
     LTQHRWLLKL AVCAVPLPWI AVEAGWLVAE FGRQPWVIEG VLPTAVAVSS LGIKTLLITL
     GGFILIYTVL FIIEMKLIFK VIHAGPSAEH SPQEMSDLKP VLAGTPAATP EQS
//
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