ID C5E8R9_BIFLI Unreviewed; 490 AA.
AC C5E8R9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000256|HAMAP-Rule:MF_01347,
GN ECO:0000313|EMBL:EEQ54413.1};
GN ORFNames=BLIG_00363 {ECO:0000313|EMBL:EEQ54413.1};
OS Bifidobacterium longum subsp. infantis CCUG 52486.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=537937 {ECO:0000313|EMBL:EEQ54413.1};
RN [1] {ECO:0000313|EMBL:EEQ54413.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 52486 {ECO:0000313|EMBL:EEQ54413.1};
RG The Broad Institute Genome Sequencing Platform;
RA Gougoulias C., Tuohy K.M., Gibson G.R., Ward D., Mehta T., Young S.,
RA Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., Sykes S.,
RA Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J., Nusbaum C.,
RA Birren B.;
RT "Annotation of Bifidobacterium longum subsp. infantis CCUG 52486.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
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:0000256|HAMAP-Rule:MF_01347};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01347};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01347}.
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DR EMBL; DS990238; EEQ54413.1; -; Genomic_DNA.
DR RefSeq; WP_007051478.1; NZ_DS990238.1.
DR AlphaFoldDB; C5E8R9; -.
DR SMR; C5E8R9; -.
DR GeneID; 69577499; -.
DR HOGENOM; CLU_022398_0_2_11; -.
DR Proteomes; UP000005084; Unassembled WGS sequence.
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 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; IPR005722; ATP_synth_F1_bsu.
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; 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 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 {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01347};
KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01347};
KW Hydrolase {ECO:0000313|EMBL:EEQ54413.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01347};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01347}.
FT DOMAIN 165..369
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 173..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ SEQUENCE 490 AA; 53310 MW; 1255513A1E76FB92 CRC64;
MADNQTTAAE PTNGRVTRVQ GSVIDVEFPV GHLPDIYNAL KVTIVNTSAK EEGEAKETEI
TLEVEQHLGD STVRCVALKP TDGLVRGASV SDTGAPISVP VGDVTKGHVF DVSGNILNKK
PDETITVSER WPIHRNPPAF DQLESKTQMF ETGIKVIDLL TPYVQGGKIG LFGGAGVGKT
VLIQEMIQRV AQNHGGVSVF AGVGERTREG NDLIGEMAEA GVLEKTALVF GQMDEQPGTR
LRVPLTALTM AEYFRDVQNQ DVLLFIDNIF RFTQAGSEVS TLLGRMPSAV GYQPNLADEM
GSLQERITST RGHSITSLQA IYVPADDYTD PAPATTFAHL DATTELSRDI ASKGIYPAVD
PLSSTSRILD PRYVGQAHYD CANRVKAILQ RNKELQDIIA LIGIDELGEE DKTTVNRARK
IEQFLGQNFY VAEKFTGRPG SYVPADETIE AFTRICDGVY DDVPEQAFSG IGGIDDLEEK
WHNMQKELGA
//
