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Database: UniProt
Entry: C1KRF2_MICCC
LinkDB: C1KRF2_MICCC
Original site: C1KRF2_MICCC 
ID   C1KRF2_MICCC            Unreviewed;       215 AA.
AC   C1KRF2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=ATP synthase protein MI25 {ECO:0000256|ARBA:ARBA00017388};
GN   Name=atp4_1 {ECO:0000313|EMBL:ACO55584.1};
GN   Synonyms=atp4_2 {ECO:0000313|EMBL:ACO55602.1};
GN   ORFNames=MicpuN_mit46 {ECO:0000313|EMBL:ACO55602.1}, MicpuN_mit6
GN   {ECO:0000313|EMBL:ACO55584.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OG   Mitochondrion {ECO:0000313|EMBL:ACO55584.1}.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO55584.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO55584.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 {ECO:0000313|EMBL:ACO55584.1}, and RCC299 / NOUM17
RC   {ECO:0000313|Proteomes:UP000002009};
RG   Micromonas genome consortium;
RA   Robbens S., Rombauts S., Lucas S., Glavina del Rio T., Tice H., Bruce D.,
RA   Pitluck S., Van de Peer Y., Zhou K., Grimwood J., Grigoriev I.V.,
RA   Cuvelier M.L., Worden A.Z.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACO55584.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 {ECO:0000313|EMBL:ACO55584.1}, and RCC299 / NOUM17
RC   {ECO:0000313|Proteomes:UP000002009};
RA   Worden A.Z., Lee J.-H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Schnitzler Parker M., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.X., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This is one of the chains of the nonenzymatic component
CC       (CF(0) subunit) of the mitochondrial ATPase complex.
CC       {ECO:0000256|ARBA:ARBA00003096}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a, b and c. {ECO:0000256|ARBA:ARBA00011648}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       membrane {ECO:0000256|ARBA:ARBA00004304}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004304}.
CC   -!- SIMILARITY: Belongs to the ATPase protein MI25 family.
CC       {ECO:0000256|ARBA:ARBA00009281}.
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DR   EMBL; FJ859351; ACO55584.1; -; Genomic_DNA.
DR   EMBL; FJ859351; ACO55602.1; -; Genomic_DNA.
DR   RefSeq; YP_002860120.1; NC_012643.1.
DR   RefSeq; YP_002860138.1; NC_012643.1.
DR   AlphaFoldDB; C1KRF2; -.
DR   STRING; 296587.C1KRF2; -.
DR   GeneID; 7804319; -.
DR   GeneID; 7804358; -.
DR   KEGG; mis:MicpuN_mit46; -.
DR   KEGG; mis:MicpuN_mit6; -.
DR   InParanoid; C1KRF2; -.
DR   OMA; VICAKQI; -.
DR   OrthoDB; 1214612at2759; -.
DR   Proteomes; UP000002009; Mitochondrion.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR   InterPro; IPR044988; MI25_plants.
DR   PANTHER; PTHR37774:SF4; ATP SYNTHASE PROTEIN MI25; 1.
DR   PANTHER; PTHR37774; ATP SYNTHASE PROTEIN MI25-RELATED; 1.
DR   Pfam; PF05405; Mt_ATP-synt_B; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000313|EMBL:ACO55584.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        33..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          191..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   215 AA;  24427 MW;  30C5D8C3F85A0977 CRC64;
     MQMIQQNLAY ILGGTLLFLV CSSKNILIYN EELLIALSFL AFIATSAHTM GDAIAETFQT
     RADQIQTELQ AFFVAKETLY HEVKHQIQMQ QTLAQSMTAL GTLVQHQLQD LHTQRAKALQ
     NSVQTRTVTQ LQHMVSQQNA VHAHLHNVTS QTYTHVMLEA IQLQKQHMQK LCMENALQLL
     GTMKRKNVTQ KQIDTKKVES TQNTVKKTGN KTKKK
//
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