ID Q6RX84_BIFLI Unreviewed; 373 AA.
AC Q6RX84;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=ATP synthase beta chain {ECO:0000313|EMBL:AAR27805.1};
DE Flags: Fragment;
GN Name=atpD {ECO:0000313|EMBL:AAR27805.1};
OS Bifidobacterium longum subsp. infantis.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1682 {ECO:0000313|EMBL:AAR27805.1};
RN [1] {ECO:0000313|EMBL:AAR27805.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 15697 {ECO:0000313|EMBL:AAR27805.1};
RX PubMed=15128574; DOI=10.1128/AEM.70.5.3110-3121.2004;
RA Ventura M., Canchaya C., van Sinderen D., Fitzgerald G.F., Zink R.;
RT "Bifidobacterium lactis DSM 10140: identification of the atp (atpBEFHAGDC)
RT operon and analysis of its genetic structure, characteristics, and
RT phylogeny.";
RL Appl. Environ. Microbiol. 70:3110-3121(2004).
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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DR EMBL; AY487150; AAR27805.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6RX84; -.
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-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 3.40.50.12240; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-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};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 88..337
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAR27805.1"
FT NON_TER 373
FT /evidence="ECO:0000313|EMBL:AAR27805.1"
SQ SEQUENCE 373 AA; 40653 MW; 433F2C9728D654FA CRC64;
LKPTDGLVRG ASVSDTGVPI SVPVGDVTKG HVFDVSGNIL NKKPDETITV SERWPIHRNP
PAFDQLESKT QMFETGIKVI DLLTPYVQGG KIGLFGGAGV GKTVLIQEMI QRVAQNHGGV
SVFAGVGERT REGNDLIGEM AEAGVLEKTA LVFGQMDEQP GTRLRVPLTA LTMAEYFRDV
QNQDVLLFID NIFRFTQAGS EVSTLLGRMP SAVGYQPNLA DEMGSLQERI TSTRGHSITS
LQAIYVPADD YTDPAPATTF AHLDATTELS RDIASKGIYP AVDPLSSTSR ILDPRYVGQA
HYDCANRVKA ILQRNKELQD IIALIGIDEL SEEDKTTVNR ARKIEQFLGQ NFYVAEKFTG
RPGSYVPADE TIE
//
