ID A0A9D3PZL5_MEGAT Unreviewed; 252 AA.
AC A0A9D3PZL5;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 9.
DE RecName: Full=ATP synthase subunit b {ECO:0000256|RuleBase:RU368017};
GN ORFNames=MATL_G00109500 {ECO:0000313|EMBL:KAG7472506.1};
OS Megalops atlanticus (Tarpon) (Clupea gigantea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Elopiformes; Megalopidae; Megalops.
OX NCBI_TaxID=7932 {ECO:0000313|EMBL:KAG7472506.1, ECO:0000313|Proteomes:UP001046870};
RN [1] {ECO:0000313|EMBL:KAG7472506.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YG-15Mar2019-1 {ECO:0000313|EMBL:KAG7472506.1};
RC TISSUE=Brain {ECO:0000313|EMBL:KAG7472506.1};
RA Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA Lampietro C., Louis A., Herpin A., Echchiki A., Berthelot C., Parey E.,
RA Roest-Crollius H., Braasch I., Postlethwait J., Bobe J., Montfort J.,
RA Bouchez O., Begum T., Mejri S., Adams A., Chen W.-J., Guiguen Y.;
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit b, of the mitochondrial membrane ATP synthase complex
CC (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the
CC presence of a proton gradient across the membrane which is generated by
CC electron transport complexes of the respiratory chain. ATP synthase
CC complex consist of a soluble F(1) head domain - the catalytic core
CC - and a membrane F(1) domain - the membrane proton channel. These two
CC domains are linked by a central stalk rotating inside the F(1) region
CC and a stationary peripheral stalk. During catalysis, ATP synthesis in
CC the catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. In vivo, can only
CC synthesize ATP although its ATP hydrolase activity can be activated
CC artificially in vitro. Part of the complex F(0) domain. Part of the
CC complex F(0) domain and the peripheric stalk, which acts as a stator to
CC hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements. {ECO:0000256|ARBA:ARBA00055529,
CC 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(1) and CF(0) have
CC multiple subunits. {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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG7472506.1}.
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DR EMBL; JAFDVH010000008; KAG7472506.1; -; Genomic_DNA.
DR OrthoDB; 67388at2759; -.
DR Proteomes; UP001046870; Chromosome 8.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:TreeGrafter.
DR FunFam; 1.20.5.2210:FF:000003; ATP synthase subunit B; 1.
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:UP001046870};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368017}.
SQ SEQUENCE 252 AA; 28082 MW; 18112D34C85FE658 CRC64;
MLSRLVLVSG SALKSRGALG AGLLQASRSL HASPQSLAPV PPLPEKGGKV RHGIIPEELF
QFLYPKTGVT GPYMLGTGLL LYLLSKEIYV INHETFAAAS IGIVIVYGIK KFGPSVAAFA
DKLNEEKVAK VQEVKDLATS SLTQAIEQEK KEQWRAEGRQ MLFDAKRNNV VMLLETNHRE
RLHMVTNEVK KRLDYQIALQ NLHRRMEQEH MVDWVEKNVI KSITPQQEKE SIAKCITDLK
MLAKATQAKA TA
//
