ID ATPB1_CHLTE Reviewed; 480 AA.
AC Q8KDL4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-NOV-2024, entry version 133.
DE RecName: Full=ATP synthase subunit beta 1 {ECO:0000255|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta 1 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta 1 {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD1 {ECO:0000255|HAMAP-Rule:MF_01347}; OrderedLocusNames=CT1033;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The catalytic sites are hosted primarily by the
CC beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out);
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01347};
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 four main
CC subunits: a(1), b(1), b'(1) and c(9-12). {ECO:0000255|HAMAP-
CC Rule:MF_01347}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; AE006470; AAM72266.1; -; Genomic_DNA.
DR RefSeq; NP_661924.1; NC_002932.3.
DR RefSeq; WP_010932711.1; NC_002932.3.
DR AlphaFoldDB; Q8KDL4; -.
DR SMR; Q8KDL4; -.
DR STRING; 194439.CT1033; -.
DR EnsemblBacteria; AAM72266; AAM72266; CT1033.
DR KEGG; cte:CT1033; -.
DR PATRIC; fig|194439.7.peg.941; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_10; -.
DR OrthoDB; 9801639at2; -.
DR Proteomes; UP000001007; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR FunFam; 1.10.1140.10:FF:000006; ATP synthase subunit beta; 1.
DR FunFam; 3.40.50.300:FF:001630; ATP synthase subunit beta; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR017691; Alt_ATPase_F1_bsu.
DR InterPro; IPR055190; ATP-synt_VA_C.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR050053; ATPase_alpha/beta_chains.
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 NCBIfam; TIGR03305; alt_F1F0_F1_bet; 1.
DR NCBIfam; TIGR01039; atpD; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF22919; ATP-synt_VA_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1);
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..480
FT /note="ATP synthase subunit beta 1"
FT /id="PRO_0000339511"
FT BINDING 154..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 480 AA; 52608 MW; ED55C213D2764BAE CRC64;
MGKTEPEQTG IVTSIRGSVV DMRFDELLPS IYSVVKTGRE MEVTVEILMQ LDRRHVRGIA
LTPTEGLCRG MKARNTGSPL KAPVGKGTLS RMFDVFGNAI DRRGPVTNVT WRSVHGAPPQ
LSRRSTKSEV FETGIKIIDL LVPLERGGKA GLFGGAGVGK TVLLTEMIHN MVSKESGVSI
FCGIGERCRE GEELYRDMSE AGVLDNMVMV FGQMNEPPGS RFRVGLTALT MAEYFRDDLH
QEVLLLIDNI FRFIQAGSEI SGMIGQMPSR LGYQPTIGTE LSALEERIAN TGTGAITSIQ
AVYVPADDFT DPAAVHTFSH LSASLVLSRK RAGEGFYPAV DPLSSGSKMA GESIVGRRHY
DLAREVRRVL AQYAELKDII AMLGLEQLSA EDRRLVGRAR RLERFFTQPF FTTEQFSGLA
GKSVPIANTI DGCERILRDE FENYPERALY MIGSIAEAQE KTVIETTMSE SVAAKPEGGN
//
