ATPF_MYCS5
ID ATPF_MYCS5 Reviewed; 193 AA.
AC Q4A600;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 90.
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=MS53_0409;
OS Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=262723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=53;
RX PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT "Swine and poultry pathogens: the complete genome sequences of two strains
RT of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL J. Bacteriol. 187:5568-5577(2005).
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; AE017245; AAZ43821.2; -; Genomic_DNA.
DR RefSeq; WP_050703138.1; NC_007294.1.
DR AlphaFoldDB; Q4A600; -.
DR SMR; Q4A600; -.
DR STRING; 262723.MS53_0409; -.
DR EnsemblBacteria; AAZ43821; AAZ43821; MS53_0409.
DR KEGG; msy:MS53_0409; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_4_3_14; -.
DR OMA; IKSKYYM; -.
DR Proteomes; UP000000549; 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..193
FT /note="ATP synthase subunit b"
FT /id="PRO_0000368616"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 193 AA; 22069 MW; 4D61FB9A068BAE95 CRC64;
MSSSVQVLSE TIEIGKVVTA SDEIAKRFNN LFPSIPMMLA TFIAFVIVFL LLFFFLYNPV
KKMIRKRQEF IQSQIDDSIK AKEDSLAKLS QAQAELIESH KQSVNIVNNA KSKAQEILAS
YKNKAISDAN RLIEETQIDL NERKKEFDKN SRILIAETAT EIAQRILKRE ISKSTQDEII
KDFLEDKTPI EDI
