ATP6_LIMF3
ID ATP6_LIMF3 Reviewed; 236 AA.
AC B2GAT9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; OrderedLocusNames=LAF_0435;
OS Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS fermentum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=334390;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3956 / LMG 18251;
RX PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA Hattori M.;
RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT fermentum reveal a genomic island for reuterin and cobalamin production.";
RL DNA Res. 15:151-161(2008).
CC -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC in the translocation of protons across the membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(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_01393}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01393};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
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DR EMBL; AP008937; BAG26771.1; -; Genomic_DNA.
DR RefSeq; WP_003682740.1; NC_010610.1.
DR AlphaFoldDB; B2GAT9; -.
DR SMR; B2GAT9; -.
DR EnsemblBacteria; BAG26771; BAG26771; LAF_0435.
DR GeneID; 61201072; -.
DR KEGG; lfe:LAF_0435; -.
DR eggNOG; COG0356; Bacteria.
DR HOGENOM; CLU_041018_2_3_9; -.
DR OMA; FTHAVRL; -.
DR OrthoDB; 867266at2; -.
DR Proteomes; UP000001697; 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 Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR42823; PTHR42823; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..236
FT /note="ATP synthase subunit a"
FT /id="PRO_1000145282"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ SEQUENCE 236 AA; 26271 MW; FB0D26D46C6A68FE CRC64;
MGGDAFTFEL FGLTFNWTNL ISGTIVFVIT FFLLFGLSRH LQMKPTGGQN VLEWIVEFTN
GIVRGQMPSE TSGFYSFFVF VLFVFLFISN QLGLIIQFGW NGHEIVKSPT ADPVVTMTLA
LCAVTLSHFA GVARQGVKGY FADYFKPFSL MFPIKLVEEF SNFLTLGLRI FGNIYAGELL
LKLLAGMAFS HGIPTMIVSL PLEIIWQGFS VFIGAIQAYV FVTLTTVYIS RKVTGE