YTHA_BACSU
ID YTHA_BACSU Reviewed; 443 AA.
AC C0SP90; O34655; Q795N7;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Putative cytochrome bd menaquinol oxidase subunit I;
DE EC=1.10.3.-;
GN Name=ythA; OrderedLocusNames=BSU30710;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP DISCUSSION OF SEQUENCE.
RX PubMed=9852001; DOI=10.1128/jb.180.24.6571-6580.1998;
RA Winstedt L., Yoshida K.-I., Fujita Y., von Wachenfeldt C.;
RT "Cytochrome bd biosynthesis in Bacillus subtilis: characterization of the
RT cydABCD operon.";
RL J. Bacteriol. 180:6571-6580(1998).
RN [4]
RP FUNCTION IN SPORULATION.
RX PubMed=11073895; DOI=10.1128/jb.182.23.6557-6564.2000;
RA Winstedt L., von Wachenfeldt C.;
RT "Terminal oxidases of Bacillus subtilis strain 168: one quinol oxidase,
RT cytochrome aa(3) or cytochrome bd, is required for aerobic growth.";
RL J. Bacteriol. 182:6557-6564(2000).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=17114254; DOI=10.1128/jb.01381-06;
RA Thomaides H.B., Davison E.J., Burston L., Johnson H., Brown D.R.,
RA Hunt A.C., Errington J., Czaplewski L.;
RT "Essential bacterial functions encoded by gene pairs.";
RL J. Bacteriol. 189:591-602(2007).
CC -!- FUNCTION: May have a role in sporulation. Can compensate for the loss
CC of cytochrome aa3. {ECO:0000269|PubMed:11073895}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 protoheme IX group (heme b). {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Not essential. {ECO:0000269|PubMed:17114254}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 1
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00371.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF008220; AAC00371.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15049.2; -; Genomic_DNA.
DR RefSeq; NP_390949.2; NC_000964.3.
DR RefSeq; WP_004399130.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; C0SP90; -.
DR SMR; C0SP90; -.
DR STRING; 224308.BSU30710; -.
DR PaxDb; C0SP90; -.
DR PRIDE; C0SP90; -.
DR EnsemblBacteria; CAB15049; CAB15049; BSU_30710.
DR GeneID; 937142; -.
DR KEGG; bsu:BSU30710; -.
DR PATRIC; fig|224308.179.peg.3329; -.
DR eggNOG; COG1271; Bacteria.
DR InParanoid; C0SP90; -.
DR OMA; GWIFACT; -.
DR PhylomeDB; C0SP90; -.
DR BioCyc; BSUB:BSU30710-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0070069; C:cytochrome complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IBA:GO_Central.
DR GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Sporulation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..443
FT /note="Putative cytochrome bd menaquinol oxidase subunit I"
FT /id="PRO_0000389495"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 182
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"
SQ SEQUENCE 443 AA; 49213 MW; DD3256331B281CDC CRC64;
MDDLVLARSL FGTTMGFHII FATLGVGLPL MILVAELIYQ KTKDDHYAIM AKRWTKAQAV
LLGVAIPTGT IAGTQLALLW PGFMEVIGRV MSLPFQIEIY AFFVEALFMS IYVYAADRLS
PAMRIVAVFF VLVGAAASAV LITNVHAFEG TPAGFKILNG KITDVDPWAA FFNPSFFITA
GHVVLSAFMT GAFIVASVAA YKMIRTRKKE RVYRFHRKAL LLALTIGGIF SLLTALNGHE
SAQMLYEYQP EKLAGAEGLF ETRSHAPLAI GGFTDPNEEK VKWAIEIPWA LSFLAANRFD
TVVKGLNAFP RDEWPPLFIH TLFNAMVGVG MLLILYSIIG VVWRKVLKKD RFPTWLLIIF
MTAGPFSLIG IEFGWIFACT GRQPWVIYHL LKTSDVVTTT GSIGVLFLFF TFVYAVLGAA
VVYVLLYYFR KHPVDEDLNT AES
