ATPB_ACEWD
ID ATPB_ACEWD Reviewed; 466 AA.
AC P50002; H6LG96;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=ATP synthase subunit beta, sodium ion specific;
DE EC=7.2.2.1;
DE AltName: Full=Na(+)-translocating ATPase subunit beta;
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; Synonyms=uncD;
GN OrderedLocusNames=Awo_c02230;
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=931626;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX PubMed=7748890; DOI=10.1016/0005-2728(95)00037-j;
RA Forster A., Daniel R., Mueller V.;
RT "The Na(+)-translocating ATPase of Acetobacterium woodii is a F1F0-type
RT enzyme as deduced from the primary structure of its beta, gamma and epsilon
RT subunits.";
RL Biochim. Biophys. Acta 1229:393-397(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT "Complete genome sequence of Acetobacterium woodii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-9, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX PubMed=8033902; DOI=10.1111/j.1432-1033.1994.tb18992.x;
RA Reidlinger J., Mueller V.;
RT "Purification of ATP synthase from Acetobacterium woodii and identification
RT as a Na(+)-translocating F1F0-type enzyme.";
RL Eur. J. Biochem. 223:275-283(1994).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a sodium ion
CC gradient across the membrane. The beta chain is the catalytic subunit.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + 4 Na(+)(in) = ADP + H(+) + 4 Na(+)(out) +
CC phosphate; Xref=Rhea:RHEA:58156, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.1;
CC -!- ACTIVITY REGULATION: Inhibited by nitrate.
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, b and c. {ECO:0000269|PubMed:8033902}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01347,
CC ECO:0000269|PubMed:8033902}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01347, ECO:0000269|PubMed:8033902}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; U10505; AAA79908.1; -; Genomic_DNA.
DR EMBL; CP002987; AFA47032.1; -; Genomic_DNA.
DR PIR; I39748; I39748.
DR RefSeq; WP_014354635.1; NC_016894.1.
DR AlphaFoldDB; P50002; -.
DR SMR; P50002; -.
DR STRING; 931626.Awo_c02230; -.
DR TCDB; 3.A.2.1.5; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR EnsemblBacteria; AFA47032; AFA47032; Awo_c02230.
DR KEGG; awo:Awo_c02230; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_9; -.
DR OMA; GFNMIMD; -.
DR OrthoDB; 430176at2; -.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046932; F:sodium-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046962; F:sodium-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; Cell membrane; CF(1);
KW Direct protein sequencing; Ion transport; Membrane; Nucleotide-binding;
KW Reference proteome; Sodium; Sodium transport; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8033902"
FT CHAIN 2..466
FT /note="ATP synthase subunit beta, sodium ion specific"
FT /id="PRO_0000144413"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 303
FT /note="V -> D (in Ref. 1; AAA79908)"
FT /evidence="ECO:0000305"
FT CONFLICT 404..425
FT /note="FLSQPFNVAEQFTGTAGVYVTI -> LFANHLMLRNSLPVRWGICKRF (in
FT Ref. 1; AAA79908)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="E -> Q (in Ref. 1; AAA79908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 50663 MW; 706CAAE301FC126A CRC64;
MAQNIGKVVQ VIGPVVDVKF QKDKLPKLNN AVNIELNGHT LVIEVAQQLG DDIVRCIAMD
STDGLMRNQE AVDTGSAIQV PVGKATLGRM FNVLGEPIDG KPFDTKDVVM HPIHRHPPSF
EEQQTQPEMF ETGIKVVDLI CPYVRGGKIG LFGGAGVGKT VLIQELINNI ATQHGGLSVF
AGVGERTREG NDLYYEMMES GVINKTALCF GQMNEPPGAR MRIALAGLTM AEYFRDDEGQ
DVLLFIDNIF RFTQAGSEVS ALLGRMPSAV GYQPTLATEM GALQERITST SKGSITSVQA
VYVPADDLTD PAPATTFAHL DATTVLSRAI TEKGIYPAVD PLDSTSRILD PKIVGQEHYE
TAREVQEILQ RYKELQDIIA ILGMDELSDA DKITVSRARK VERFLSQPFN VAEQFTGTAG
VYVTIGDTIK GFKEILEGQH DDLPESAFLL VGTIEDAVVK AKKIKG
