ID D0MST8_PHYIT Unreviewed; 308 AA.
AC D0MST8;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=ATP synthase subunit b {ECO:0000256|RuleBase:RU368017};
GN ORFNames=PITG_00074 {ECO:0000313|EMBL:EEY57522.1};
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY57522.1, ECO:0000313|Proteomes:UP000006643};
RN [1] {ECO:0000313|Proteomes:UP000006643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Part of the complex
CC F(0) domain and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements. {ECO:0000256|RuleBase:RU368017}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(0) has three main
CC subunits: a, b and c. {ECO:0000256|RuleBase:RU368017}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU368017}.
CC Mitochondrion inner membrane {ECO:0000256|RuleBase:RU368017}.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC {ECO:0000256|RuleBase:RU368017}.
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DR EMBL; DS028118; EEY57522.1; -; Genomic_DNA.
DR RefSeq; XP_002908708.1; XM_002908662.1.
DR AlphaFoldDB; D0MST8; -.
DR STRING; 403677.D0MST8; -.
DR EnsemblProtists; PITG_00074T0; PITG_00074T0; PITG_00074.
DR GeneID; 9476594; -.
DR KEGG; pif:PITG_00074; -.
DR VEuPathDB; FungiDB:PITG_00074; -.
DR eggNOG; ENOG502RU2Z; Eukaryota.
DR HOGENOM; CLU_059114_0_0_1; -.
DR InParanoid; D0MST8; -.
DR OMA; DWKISMP; -.
DR OrthoDB; 38103at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-UniRule.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:UniProtKB-UniRule.
DR InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR InterPro; IPR013837; ATP_synth_F0_suB.
DR PANTHER; PTHR12733:SF3; ATP SYNTHASE F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12733; MITOCHONDRIAL ATP SYNTHASE B CHAIN; 1.
DR Pfam; PF05405; Mt_ATP-synt_B; 1.
DR SUPFAM; SSF161060; ATP synthase B chain-like; 1.
PE 3: Inferred from homology;
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU368017};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU368017};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU368017};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368017};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU368017};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|RuleBase:RU368017};
KW Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
SQ SEQUENCE 308 AA; 33921 MW; 5E6E818B3943CCC8 CRC64;
MLGRIALRKA ALSSSKLSSA KMMRPMGLHT TGVVRKNEEA SEEIQVPTQG LLEQAGLTDW
KISAPIIGAL AIPAISNHFY VLNEESQLAC CFLLFCSASY KFGGEMIASY FDERAAAILG
EHNAVEDANL DLAKETLETH KALLNIHEDI AAVAEAHKEA VALMCEVQAY KLRHKTRETF
VKNLESIREI EGSYNLELQK SMVASATSKV RTVVQKGDKK LKDAAFKHAL DILGNANVDD
SKEDDVAALF TKELRAYASD LEAKQGQVVK LTAEEQSELQ ADLDAYMNRF GLEDADFKAP
KEVKLELM
//
