ID A0A075AIV4_9TREM Unreviewed; 318 AA.
AC A0A075AIV4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=ATP synthase subunit b {ECO:0000256|RuleBase:RU368017};
DE Flags: Fragment;
GN ORFNames=T265_12840 {ECO:0000313|EMBL:KER32289.1}, X801_04987
GN {ECO:0000313|EMBL:OON19149.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER32289.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER32289.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OON19149.1, ECO:0000313|Proteomes:UP000243686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Khon Kaen {ECO:0000313|EMBL:OON19149.1};
RA Mitreva M.;
RT "Draft genome of the nematode, Opisthorchis viverrini.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00007479, ECO:0000256|RuleBase:RU368017}.
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DR EMBL; KL596636; KER32289.1; -; Genomic_DNA.
DR EMBL; KV893553; OON19149.1; -; Genomic_DNA.
DR RefSeq; XP_009164065.1; XM_009165801.1.
DR AlphaFoldDB; A0A075AIV4; -.
DR STRING; 6198.A0A075AIV4; -.
DR GeneID; 20327008; -.
DR KEGG; ovi:T265_12840; -.
DR CTD; 20327008; -.
DR OrthoDB; 2939076at2759; -.
DR Proteomes; UP000054324; Unassembled WGS sequence.
DR Proteomes; UP000243686; Unassembled 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 Gene3D; 1.20.5.2210; -; 1.
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:UP000054324};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KER32289.1"
SQ SEQUENCE 318 AA; 36279 MW; F2B600A05C773225 CRC64;
DKVLGELEAT ALLLNRVPRP NGFAVWTFVV SLVGHKGSNL LYSAARSRTA SSVTTAATSD
LEKYVKKSEE LASKYEKHVD EAVTRWAKCD EIYFGKERDF KNFPTVKYPL KHPKVRLGFI
PDAWFQTLYP ITGVTGPYLF LFGSTAFLIS KEILVVDPHF IEMGVFIVLM TGLIKKFGPL
VAEFLDKHTE KVEQIRYYEP LNALHRNLDK TIATANEEIA RASAVESLVK AKEENVALQL
EAAYRERLQQ VYRAVHRRLD YHVERENTRR RFQQTHLINW VVDQVVKGIT PAQEKETLTY
CIGELKRLAQ VHKTAAVA
//
