ATPF1_PROA2
ID ATPF1_PROA2 Reviewed; 253 AA.
AC B4S7A0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=Paes_0894;
OS Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=290512;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 271 / SK 413;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL Submitted (JUN-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 four 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner 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; CP001108; ACF45937.1; -; Genomic_DNA.
DR RefSeq; WP_012505474.1; NC_011059.1.
DR AlphaFoldDB; B4S7A0; -.
DR SMR; B4S7A0; -.
DR STRING; 290512.Paes_0894; -.
DR EnsemblBacteria; ACF45937; ACF45937; Paes_0894.
DR KEGG; paa:Paes_0894; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_070737_0_0_10; -.
DR OMA; DWFTVIA; -.
DR OrthoDB; 1456190at2; -.
DR Proteomes; UP000002725; 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; IPR017707; Alt_ATP_synth_F0_bsu.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR Pfam; PF00430; ATP-synt_B; 1.
DR TIGRFAMs; TIGR03321; alt_F1F0_F0_B; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..253
FT /note="ATP synthase subunit b 1"
FT /id="PRO_0000368675"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 253 AA; 28896 MW; 8AA1983C8C663FCE CRC64;
MLIDWFTVIA ELVNFLILVW LLKRFLYEPV LKAIDEREKK IASELQHAAD VEKEAESRLI
ELQRKNEAFD NAHAQMIKDA EQEAVEEKRT LLNEAHREYD ALRMRLQETL KHEETSLESR
VTGRISAEVF SIARKVLQDL SGSSLEAQIA DVFCQRLRES DPEDVAAMKD AVSRKSLNPL
VRSTFPLSSS LQERIQAVVR DVFSIDTQLR FEEGDDMVGG IELSMNGHSV SWSVRSYLDS
LEKMTAELLE GAE