ATPF_UREP2
ID ATPF_UREP2 Reviewed; 205 AA.
AC B1AIC4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=UPA3_0141;
OS Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=505682;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA Methe B.A., Glass J., Waites K., Shrivastava S.;
RT "Genome sequence of Ureaplasma parvum serovar 3.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000942; ACA33087.1; -; Genomic_DNA.
DR AlphaFoldDB; B1AIC4; -.
DR SMR; B1AIC4; -.
DR EnsemblBacteria; ACA33087; ACA33087; UPA3_0141.
DR KEGG; upa:UPA3_0141; -.
DR HOGENOM; CLU_079215_4_3_14; -.
DR OMA; FAWKPIL; -.
DR Proteomes; UP000002162; 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 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Lipoprotein; Membrane; Palmitate; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..205
FT /note="ATP synthase subunit b"
FT /id="PRO_0000368853"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT LIPID 28
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 28
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 205 AA; 23216 MW; 8ED70551CE7B6AD2 CRC64;
MKLNKKHLVA ILSVLSLSII VVPLLTSCTG DIPELNPAEI INTLFPNVWV FIAQVIAMCV
VFSLVLWLVW KPTNKMLDKR REYIAKEITD AENAKQEALQ YLENAKSEHL AAQAQTLEII
AKAKSESLTL RESLEKEARE AADKIISSAK ISIANERREN LERLQSEARE AAYIAAEALM
KKELSREDND KLVDQFIKEL ENNEK
