CYDA_SHIFL
ID CYDA_SHIFL Reviewed; 522 AA.
AC P0ABK1; P11026; P75754; P76823;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cytochrome bd-I ubiquinol oxidase subunit 1;
DE EC=7.1.1.7 {ECO:0000250|UniProtKB:P0ABJ9};
DE AltName: Full=Cytochrome bd-I oxidase subunit I;
DE AltName: Full=Cytochrome d ubiquinol oxidase subunit I;
GN Name=cydA; OrderedLocusNames=SF0564, S0577;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: A terminal oxidase that produces a proton motive force by the
CC vectorial transfer of protons across the inner membrane. It is the
CC component of the aerobic respiratory chain of E.coli that predominates
CC when cells are grown at low aeration. Generates a proton motive force
CC using protons and electrons from opposite sides of the membrane to
CC generate H(2)O, transferring 1 proton/electron.
CC {ECO:0000250|UniProtKB:P0ABJ9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4
CC H(+)(out) + 2 H2O(in); Xref=Rhea:RHEA:40527, Rhea:RHEA-COMP:9565,
CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.7;
CC Evidence={ECO:0000250|UniProtKB:P0ABJ9};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P0ABJ9};
CC Note=Binds 1 protoheme IX center (heme b558).
CC {ECO:0000250|UniProtKB:P0ABJ9};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P0ABJ9};
CC Note=Binds 1 protoheme IX center (heme b595) per heterodimer, in
CC conjunction with CydB. {ECO:0000250|UniProtKB:P0ABJ9};
CC -!- COFACTOR:
CC Name=heme d cis-diol; Xref=ChEBI:CHEBI:62814;
CC Evidence={ECO:0000250|UniProtKB:P0ABJ9};
CC Note=Binds 1 iron-chlorin (heme d or cytochrome d) per heterodimer, in
CC conjunction with CydB. {ECO:0000250|UniProtKB:P0ABJ9};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBUNIT: Heterodimer of subunits I and II.
CC {ECO:0000250|UniProtKB:P0ABJ9}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0ABJ9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0ABJ9}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 1
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN42208.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP16081.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN42208.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP16081.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_706501.1; NC_004337.2.
DR RefSeq; WP_000884361.1; NZ_UIPM01000010.1.
DR AlphaFoldDB; P0ABK1; -.
DR SMR; P0ABK1; -.
DR STRING; 198214.SF0564; -.
DR PRIDE; P0ABK1; -.
DR EnsemblBacteria; AAN42208; AAN42208; SF0564.
DR EnsemblBacteria; AAP16081; AAP16081; S0577.
DR GeneID; 1023517; -.
DR GeneID; 66670998; -.
DR KEGG; sfl:SF0564; -.
DR KEGG; sfx:S0577; -.
DR PATRIC; fig|198214.7.peg.654; -.
DR HOGENOM; CLU_030555_0_1_6; -.
DR OMA; FLINIAM; -.
DR OrthoDB; 271551at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0070069; C:cytochrome complex; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR InterPro; IPR002585; Cyt-d_ubiquinol_oxidase_su_1.
DR PANTHER; PTHR30365; PTHR30365; 1.
DR Pfam; PF01654; Cyt_bd_oxida_I; 1.
DR PIRSF; PIRSF006446; Cyt_quinol_oxidase_1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; Formylation; Heme;
KW Iron; Membrane; Metal-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..522
FT /note="Cytochrome bd-I ubiquinol oxidase subunit 1"
FT /id="PRO_0000183921"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..42
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 43..94
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 95..114
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 115..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 150..187
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 208..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 240..392
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 393..412
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 413..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 471..490
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 491..522
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT BINDING 19
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b595"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 186
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b558"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b558"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000250"
FT CONFLICT 339
FT /note="A -> T (in Ref. 2; AAP16081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 58205 MW; E757442068BCFCFE CRC64;
MLDIVELSRL QFALTAMYHF LFVPLTLGMA FLLAIMETVY VLSGKQIYKD MTKFWGKLFG
INFALGVATG LTMEFQFGTN WSYYSHYVGD IFGAPLAIEG LMAFFLESTF VGLFFFGWDR
LGKVQHMCVT WLVALGSNLS ALWILVANGW MQNPIASDFN FETMRMEMVS FSELVLNPVA
QVKFVHTVAS GYVTGAMFIL GISAWYMLKG RDFAFAKRSF AIAASFGMAA VLSVIVLGDE
SGYEMGDVQK TKLAAIEAEW ETQPAPAAFT LFGIPDQEEE TNKFAIQIPY ALGIIATRSV
DTPVIGLKEL MVQHEERIRN GMKAYSLLEQ LRSGSTDQAV RDQFNSMKKD LGYGLLLKRY
TPNVADATEA QIQQATKDSI PRVAPLYFAF RIMVACGFLL LAIIALSFWS VIRNRIGEKK
WLLRAALYGI PLPWIAVEAG WFVAEYGRQP WAIGEVLPTA VANSSLTAGD LIFSMVLICG
LYTLFLVAEL FLMFKFARLG PSSLKTGRYH FEQSSTTTQP AR
