ID A0A182GHQ5_AEDAL Unreviewed; 473 AA.
AC A0A182GHQ5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=ATP synthase subunit b {ECO:0000256|RuleBase:RU368017};
GN ORFNames=RP20_CCG010112 {ECO:0000313|EMBL:KXJ76220.1};
OS Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7160 {ECO:0000313|EMBL:KXJ76220.1};
RN [1] {ECO:0000313|EMBL:KXJ76220.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ76220.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ76220.1};
RX PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA Yan G., Tu Z.J., Fang X., James A.A.;
RT "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT insights into its biology, genetics, and evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN [2] {ECO:0000313|EMBL:KXJ76220.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ76220.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ76220.1};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ562293; KXJ76220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182GHQ5; -.
DR STRING; 7160.A0A182GHQ5; -.
DR VEuPathDB; VectorBase:AALC636_034082; -.
DR VEuPathDB; VectorBase:AALC636_034399; -.
DR VEuPathDB; VectorBase:AALF010112; -.
DR VEuPathDB; VectorBase:AALFPA_061666; -.
DR VEuPathDB; VectorBase:AALFPA_080073; -.
DR Proteomes; UP000249989; Unassembled WGS sequence.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-UniRule.
DR GO; GO:0005761; C:mitochondrial ribosome; IEA:InterPro.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 1.20.5.2210; -; 1.
DR Gene3D; 6.10.330.20; -; 1.
DR InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR InterPro; IPR013837; ATP_synth_F0_suB.
DR InterPro; IPR038340; MRP-L47_sf.
DR InterPro; IPR010729; Ribosomal_uL29_mit.
DR PANTHER; PTHR12733:SF3; ATP SYNTHASE F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12733; MITOCHONDRIAL ATP SYNTHASE B CHAIN; 1.
DR Pfam; PF06984; MRP-L47; 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:UP000249989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
SQ SEQUENCE 473 AA; 55363 MW; 1DF291CAB79FBE42 CRC64;
MLSRAALLAA AKKPVGLVMT RGSASATDSN RPVRAEHPGK VRMGFLPEEW FTFFYNKTGV
TGPYVFGAGL LTYLCSKEIY VMEHEYYNGL SLAIMVIYAV KKFGPAVAAY CDKEIDRIEG
EWKADRENNI QQLAQAMEDE KKEQWRAEGQ TLLMQAKKEN VALQLEAAYR ERAMTVYREV
KKRLDYQVER QNVDRRISQK HMVDWIVKNV VKSITPEQEK ETLSRCIADL GAIAARAKLS
KAIPVPTQMA RAFSVTSKRF ELMDFFDDKK NWGENEVKHG RGWNKDELRI KSNTDLHKLW
FVLLKERNML LTMEHECNEK MELFPSPERL DKVNESMKNL EDVVRERNRA YHELETGETG
ERPAKLVTNQ LGLKFYYRMF EHVIPKYANR KWNETHKFNY QGSAVHKFLR LYREKLYNVK
RKQRNRERNE VMGLLKRFPN MDRAAIAEKY PSVDIDKLLK YDKIRGNYVS SKV
//
