ATPF1_ACAM1
ID ATPF1_ACAM1 Reviewed; 186 AA.
AC B0BZL0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=ATP synthase subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=F-type ATPase subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
DE Short=F-ATPase subunit b 1 {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF1 {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=AM1_0894;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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 four main
CC subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC form an alternating ring which encloses part of the gamma chain. F(1)
CC is 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, b and b'
CC chains. {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC 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; CP000828; ABW25936.1; -; Genomic_DNA.
DR RefSeq; WP_012161506.1; NC_009925.1.
DR AlphaFoldDB; B0BZL0; -.
DR SMR; B0BZL0; -.
DR STRING; 329726.AM1_0894; -.
DR EnsemblBacteria; ABW25936; ABW25936; AM1_0894.
DR KEGG; amr:AM1_0894; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_8_1_3; -.
DR OMA; NILNWAV; -.
DR OrthoDB; 1999641at2; -.
DR Proteomes; UP000000268; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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 Pfam; PF00430; ATP-synt_B; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..186
FT /note="ATP synthase subunit b 1"
FT /id="PRO_0000368279"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 186 AA; 19993 MW; 0414CEDC68731DEB CRC64;
MGMFNWLASA GMTGFPQLAE AGGYSLNFDI LEANLVNLVI VIGLLIYFGR GFLGESLVKR
REAIETAISE AEANQEKAAA TLAEEQEKLA QAQAEAKKIL ANAQTNASKA KEQILAEAKT
EIQRIKDAGS QDTSASQERA IAEIRQRVTA MALEKVEADL KNQLGNNESA QRKLVDQSIA
LLGGNS
