ATP synthase F(0) complex subunit B1, mitochondrial (ATP synthase peripheral stalk-membrane subunit b) (ATP synthase proton-transporting mitochondrial F(0) complex subunit B1) (ATP synthase subunit b) (ATPase subunit b)
1_MLSRV 6_ VLSAA 11_ ATAAP 16_ SLKNA 21_ AFLGP 26_ GVLQA 31_ TRTFH 36_ TGQPH 41_ LVPVP 46_ PLPEY 51_ GGKVR 56_ YGLIP 61_ EEFFQ 66_ FLYPK 71_ TGVTG 76_ PYVLG 81_ TGLIL 86_ YALSK 91_ EIYVI 96_ SAETF 101_ TALSV 106_ LGVMV 111_ YGIKK 116_ YGPFV 121_ ADFAD 126_ KLNEQ 131_ KLAQL 136_ EEAKQ 141_ ASIQH 146_ IQNAI 151_ DTEKS 156_ QQALV 161_ QKRHY 166_ LFDVQ 171_ RNNIA 176_ MALEV 181_ TYRER 186_ LYRVY 191_ KEVKN 196_ RLDYH 201_ ISVQN 206_ MMRRK 211_ EQEHM 216_ INWVE 221_ KHVVQ 226_ SISTQ 231_ QEKET 236_ IAKCI 241_ ADLKL 246_ LAKKA 251_QAQPV
1: Subunit b, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (PubMed:37244256). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity)