ATPF_MYCPN
ID ATPF_MYCPN Reviewed; 207 AA.
AC Q50327;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=MPN_602;
GN ORFNames=MP240;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8604303; DOI=10.1093/nar/24.4.628;
RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.;
RT "Sequence analysis of 56 kb from the genome of the bacterium Mycoplasma
RT pneumoniae comprising the dnaA region, the atp operon and a cluster of
RT ribosomal protein genes.";
RL Nucleic Acids Res. 24:628-639(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [3]
RP CHARACTERIZATION AS A LIPOPROTEIN, DIACYLGLYCEROL AT CYS-28, AND
RP PALMITOYLATION AT CYS-28.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=9733782; DOI=10.1074/jbc.273.38.24792;
RA Pyrowolakis G., Hofmann D., Herrmann R.;
RT "The subunit b of the F0F1-type ATPase of the bacterium Mycoplasma
RT pneumoniae is a lipoprotein.";
RL J. Biol. Chem. 273:24792-24796(1998).
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; Single-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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DR EMBL; U43738; AAC43655.1; -; Genomic_DNA.
DR EMBL; U00089; AAB95888.1; -; Genomic_DNA.
DR PIR; S62845; S62845.
DR RefSeq; NP_110291.1; NC_000912.1.
DR RefSeq; WP_010874959.1; NC_000912.1.
DR AlphaFoldDB; Q50327; -.
DR SMR; Q50327; -.
DR IntAct; Q50327; 3.
DR STRING; 272634.MPN_602; -.
DR EnsemblBacteria; AAB95888; AAB95888; MPN_602.
DR GeneID; 66608713; -.
DR KEGG; mpn:MPN_602; -.
DR PATRIC; fig|272634.6.peg.665; -.
DR HOGENOM; CLU_079215_4_3_14; -.
DR OMA; FAWKPIL; -.
DR BioCyc; MetaCyc:MON-536; -.
DR BioCyc; MPNE272634:G1GJ3-977-MON; -.
DR Proteomes; UP000000808; 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; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR Pfam; PF00430; ATP-synt_B; 1.
DR TIGRFAMs; TIGR01144; ATP_synt_b; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
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..27
FT CHAIN 28..207
FT /note="ATP synthase subunit b"
FT /id="PRO_0000002632"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT LIPID 28
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:9733782"
FT LIPID 28
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000269|PubMed:9733782"
SQ SEQUENCE 207 AA; 24019 MW; C1B0DF1D66D4E853 CRC64;
MKLRATFVFK TTLVALSFAL FALFLVSCTE NVKEIKSESV INELFPNLWV FLAHLLAFVI
LLFLLLFLFW KPTQKFLNQR KALLEEQVNQ ANSLEQQAQA LLQQANQRHE NSLVVAKEIV
DQANYEALQL KSEIEKKANR QANLMIFQAR QEIEKEKRLI QEQSLKESVE LAMLAAKELI
IKKVDVKADK AFIEEFIREL EAEDDHD
