ATPB_BACFR
ID ATPB_BACFR Reviewed; 505 AA.
AC P13356; Q64UB1;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=ATP synthase subunit beta {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 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; OrderedLocusNames=BF2171;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2978296; DOI=10.1099/00221287-134-10-2815;
RA Amann R., Ludwig W., Schleifer K.H.;
RT "Beta-subunit of ATP-synthase: a useful marker for studying the
RT phylogenetic relationship of eubacteria.";
RL J. Gen. Microbiol. 134:2815-2821(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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 + 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: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 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_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; M22247; AAA22901.1; -; Genomic_DNA.
DR EMBL; AP006841; BAD48918.1; -; Genomic_DNA.
DR PIR; A46570; A46570.
DR RefSeq; WP_005787476.1; NC_006347.1.
DR RefSeq; YP_099452.1; NC_006347.1.
DR AlphaFoldDB; P13356; -.
DR SMR; P13356; -.
DR STRING; 295405.BF2171; -.
DR EnsemblBacteria; BAD48918; BAD48918; BF2171.
DR KEGG; bfr:BF2171; -.
DR PATRIC; fig|295405.11.peg.2108; -.
DR HOGENOM; CLU_022398_0_2_10; -.
DR OMA; GFNMIMD; -.
DR Proteomes; UP000002197; 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:0046961; F:proton-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 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 Translocase; Transport.
FT CHAIN 1..505
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144419"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 80
FT /note="G -> E (in Ref. 1; AAA22901)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="K -> Q (in Ref. 1; AAA22901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 55261 MW; 8D30DC74F9503FC1 CRC64;
MSQIIGHISQ VIGPVVDVYF EGTESDLILP SIHDALEIKR HNGKKLIVEV QQHIGENTVR
TVAMDSTDGL QRGMKVFPTG GPITMPVGEQ IKGRLMNVVG DSIDGMKELN RDGAYSIHRD
PPKFEDLTTV QEVLFTGIKV IDLLEPYSKG GKIGLFGGAG VGKTVLIMEL INNIAKKHNG
FSVFAGVGER TREGNDLLRE MIESGVIRYG EAFKESMEKG HWDLSKVDYN EVEKSQATLV
FGQMNEPPGA RASVALSGLT VAESFRDMGA KSGARDILFF IDNIFRFTQA GSEVSALLGR
MPSAVGYQPT LATEMGAMQE RITSTKTGSI TSVQAVYVPA DDLTDPAPAT TFTHLDATTV
LSRKITELGI YPAVDPLEST SRILDPHIVG QEHYDVAQRV KQILQRNKEL QDIISILGME
ELSDADRLVV NRARRVQRFL SQPFTVAEQF TGVPGAMVAI EDTIKGFKMI LDGEVDYLPE
PAFLNVGTIE EAIEKGKKLL EQANK
