ATPB_PARDP
ID ATPB_PARDP Reviewed; 474 AA.
AC A1B8P0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=Pden_3818;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) 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: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; CP000490; ABL71884.1; -; Genomic_DNA.
DR RefSeq; WP_011750053.1; NC_008687.1.
DR PDB; 5CDF; X-ray; 2.30 A; E=1-474.
DR PDB; 5DN6; X-ray; 3.98 A; D/E/F=1-474.
DR PDBsum; 5CDF; -.
DR PDBsum; 5DN6; -.
DR AlphaFoldDB; A1B8P0; -.
DR SMR; A1B8P0; -.
DR STRING; 318586.Pden_3818; -.
DR TCDB; 3.A.2.1.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PRIDE; A1B8P0; -.
DR EnsemblBacteria; ABL71884; ABL71884; Pden_3818.
DR KEGG; pde:Pden_3818; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_5; -.
DR OMA; GFNMIMD; -.
DR Proteomes; UP000000361; Chromosome 2.
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 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; Cell inner membrane;
KW Cell membrane; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..474
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000339561"
FT BINDING 151..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 15..23
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 157..172
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 222..243
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:5CDF"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:5CDF"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:5CDF"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 361..379
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 381..386
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 394..410
FT /evidence="ECO:0007829|PDB:5CDF"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 430..442
FT /evidence="ECO:0007829|PDB:5CDF"
FT TURN 443..447
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:5CDF"
FT HELIX 459..468
FT /evidence="ECO:0007829|PDB:5CDF"
SQ SEQUENCE 474 AA; 50339 MW; B463293E88CC90AC CRC64;
MAEANGKITQ VIGAVVDVQF DGQLPAILNA LETENNGKRL VLEVAQHLGE NTVRTIAMDA
TEGLVRGLPV KDTGGPIMVP VGDATLGRIL NVVGEPVDEG GPVEATQTRA IHQQAPDFAA
QATASEILVT GIKVIDLLAP YSKGGKIGLF GGAGVGKTVL IMELINNIAK VHSGYSVFAG
VGERTREGND LYHEMVESGV IKPDDLSKSQ VALVYGQMNE PPGARMRVAL TGLTVAEQFR
DATGTDVLFF VDNIFRFTQA GSEVSALLGR IPSAVGYQPT LATDMGAMQE RITSTKNGSI
TSIQAVYVPA DDLTDPAPAT TFAHLDATTV LSRAISELGI YPAVDPLDSN SRILDPAVVG
EEHYQVARDV QGILQKYKSL QDIIAILGMD ELSEEDKLTV ARARKIQRFL SQPFDVAKVF
TGSDGVQVPL EDTIKSFKAV VAGEYDHLPE AAFYMVGGIE DVKAKAQRLA ADAA
