ATPF_MYCGA
ID ATPF_MYCGA Reviewed; 198 AA.
AC P33256;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 129.
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};
DE Flags: Precursor;
GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=MYCGA3020;
GN ORFNames=MGA_1168;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5969Var.B;
RX PubMed=1386735; DOI=10.1042/bj2850881;
RA Rasmussen O.F., Shirvan M.H., Margalit H., Christiansen C., Rottem S.;
RT "Nucleotide sequence, organization and characterization of the atp genes
RT and the encoded subunits of Mycoplasma gallisepticum ATPase.";
RL Biochem. J. 285:881-888(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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; X64256; CAA45547.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP56652.2; -; Genomic_DNA.
DR PIR; S24335; S24335.
DR RefSeq; WP_011113543.1; NC_004829.2.
DR AlphaFoldDB; P33256; -.
DR SMR; P33256; -.
DR KEGG; mga:MGA_1168; -.
DR PATRIC; fig|233150.7.peg.336; -.
DR HOGENOM; CLU_079215_4_3_14; -.
DR OMA; IKSKYYM; -.
DR OrthoDB; 1999641at2; -.
DR Proteomes; UP000001418; 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 Pfam; PF00430; ATP-synt_B; 1.
DR SUPFAM; SSF81573; SSF81573; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..198
FT /note="ATP synthase subunit b"
FT /id="PRO_0000002630"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT LIPID 26
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 26
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 97
FT /note="F -> L (in Ref. 1; CAA45547)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="R -> L (in Ref. 1; CAA45547)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="Q -> K (in Ref. 1; CAA45547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 22801 MW; 52F371E74F5EA340 CRC64;
MWSTRVKKLL LLSFNFLIIS AIVSSCSIPE ELQAKTIVNE FFPNFWVFVA HTIALSIIIL
LGIFLLWKPT KRFLAKRSEL IQAEINNANE IKKQAQFLLD NAKKQKQNAE LQAREIINLA
TNQAYRLKND LETDAKRKAN RIIENAHAEI IKQESILKRE LEGRIVDVAL EATSTLIQKN
VAKEDHERLV NELLRNLD
