ATPF_MYCAP
ID ATPF_MYCAP Reviewed; 189 AA.
AC A5IYE1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=ATP synthase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=F-type ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE Short=F-ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=MAG3520;
OS Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS agalactiae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=347257;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA Blanchard A., Citti C.;
RT "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT bacterial genome.";
RL PLoS Genet. 3:744-758(2007).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and 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. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. F(1) is
CC attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01398};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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DR EMBL; CU179680; CAL59050.1; -; Genomic_DNA.
DR RefSeq; WP_011949525.1; NC_009497.1.
DR AlphaFoldDB; A5IYE1; -.
DR SMR; A5IYE1; -.
DR STRING; 347257.MAG3520; -.
DR EnsemblBacteria; CAL59050; CAL59050; MAG3520.
DR KEGG; maa:MAG3520; -.
DR HOGENOM; CLU_079215_4_3_14; -.
DR OMA; FAWKPIL; -.
DR Proteomes; UP000007065; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR Pfam; PF00430; ATP-synt_B; 1.
DR SUPFAM; SSF81573; SSF81573; 1.
DR TIGRFAMs; TIGR01144; ATP_synt_b; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..189
FT /note="ATP synthase subunit b"
FT /id="PRO_0000368606"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 189 AA; 21810 MW; 02658F9D7FE806A4 CRC64;
MNLFYNLSLK ANTLLSAQSG GIKDELKDKF KTLFPTWPMF LATLIAFILV VLILWFLLHK
PIKKAMKARQ DYIQKNIDEA KLTNDISKQK LNEANKRLAE AYSEADELIK NAKIHGESVI
DEYTHKAKNK SKRIIEKAHM EIESERQKMV DDSKSNIAKA AIEISKKIMQ KEVTKESQDE
VIKNFLKDK
