ATPF_LACAC
ID ATPF_LACAC Reviewed; 169 AA.
AC Q9RGY5; Q5FKY4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=LBA0774;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ACTIVITY REGULATION, INDUCTION, AND
RP PROBABLE OPERON.
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=10510230; DOI=10.1046/j.1365-2958.1999.01557.x;
RA Kullen M.J., Klaenhammer T.R.;
RT "Identification of the pH-inducible, proton-translocating F1F0-ATPase
RT (atpBEFHAGDC) operon of Lactobacillus acidophilus by differential display:
RT gene structure, cloning and characterization.";
RL Mol. Microbiol. 33:1152-1161(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(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 -!- ACTIVITY REGULATION: Increases 2-fold following exposure to low pH.
CC {ECO:0000269|PubMed:10510230}.
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 -!- INDUCTION: By low pH. {ECO:0000269|PubMed:10510230}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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DR EMBL; AF098522; AAF22494.1; -; Genomic_DNA.
DR EMBL; CP000033; AAV42640.1; -; Genomic_DNA.
DR RefSeq; WP_003546741.1; NC_006814.3.
DR RefSeq; YP_193671.1; NC_006814.3.
DR AlphaFoldDB; Q9RGY5; -.
DR SMR; Q9RGY5; -.
DR STRING; 272621.LBA0774; -.
DR PRIDE; Q9RGY5; -.
DR EnsemblBacteria; AAV42640; AAV42640; LBA0774.
DR GeneID; 56942401; -.
DR KEGG; lac:LBA0774; -.
DR PATRIC; fig|272621.13.peg.736; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_4_2_9; -.
DR OMA; FAWKPIL; -.
DR BioCyc; LACI272621:G1G49-790-MON; -.
DR Proteomes; UP000006381; 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.
PE 2: Evidence at transcript level;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..169
FT /note="ATP synthase subunit b"
FT /id="PRO_0000368537"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 169 AA; 18589 MW; 6F618D58CA9A4C6E CRC64;
MTIQTLFAAS HHIYLGNAIW YLLCFAILML LIKHYAWGPV SDMMEKRRQK IISDLDSAAS
DRKKAETLAN EREAALKNSR QEATQILSDA KTNAQNTSKE IVASANEDAA AIRKKANEEA
AKAKSDALDA ARDQVADISV AIAEKVIAKN LSAEDQKDLV DQFIKGLDD
