(data stored in ACNUC7421 zone)

HOGENOM: FRASN_1_PE1011

ID   FRASN_1_PE1011                       STANDARD;      PRT;   479 AA.
AC   FRASN_1_PE1011; A8L3W5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP synthase subunit beta; EC=3.6.3 14;AltName: Full=ATP
DE   synthase F1 sector subunit beta;AltName: Full=F-ATPase subunit beta;
DE   (FRASN_1.PE1011).
GN   Name=atpD; OrderedLocusNames=Franean1_1024;
OS   FRANKIA SP. EAN1PEC.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Frankineae;
OC   Frankiaceae; Frankia.
OX   NCBI_TaxID=298653;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FRASN_1.PE1011.
CC       Frankia sp. EAN1pec, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:ATPB_FRASN
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton
CC       gradient across the membrane. The catalytic sites are hosted
CC       primarily by the beta subunits (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out).
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a(1), b(2) and c(9-12). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. CF(1) is attached to CF(0) by a central stalk formed
CC       by the gamma and epsilon chains, while a peripheral stalk is
CC       formed by the delta and b chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC   -!- GENE_FAMILY: HOG000009605 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A8L3W5; -.
DR   EMBL; CP000820; ABW10480.1; -; Genomic_DNA.
DR   RefSeq; YP_001505386.1; NC_009921.1.
DR   ProteinModelPortal; A8L3W5; -.
DR   SMR; A8L3W5; 19-479.
DR   STRING; A8L3W5; -.
DR   GeneID; 5669438; -.
DR   GenomeReviews; CP000820_GR; Franean1_1024.
DR   KEGG; fre:Franean1_1024; -.
DR   OMA; IGQEHYD; -.
DR   ProtClustDB; PRK09280; -.
DR   BioCyc; FSP1855:FRANEAN1_1024-MON; -.
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-KW.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1; -.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR005722; ATPase_F1-cplx_bsu.
DR   InterPro; IPR018118; ATPase_F1/A1-cplx_a/bsu_N.
DR   InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR   InterPro; IPR004100; ATPase_F1/V1/A1-cplx_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1_bsu/V1_C.
DR   Gene3D; G3DSA:1.10.1140.10; G3DSA:1.10.1140.10; 1.
DR   PANTHER; PTHR15184:SF8; ATPase_F1_b; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47917; ATPase_a/b_C; 1.
DR   SUPFAM; SSF50615; ATPase_a/b_N; 1.
DR   TIGRFAMs; TIGR01039; AtpD; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; FALSE_NEG.
DR   HOGENOMDNA; FRASN_1.PE1011; -.
KW   F0F1 ATP synthase subunit beta;
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1); Complete proteome;
KW   Hydrogen ion transport; Hydrolase; Ion transport; Membrane;
KW   Nucleotide-binding; Transport.
SQ   SEQUENCE   479 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTVTTSSPTT AEGRTPGIGR VARVIGPVVD VEFAPDELPE IYTALHVDRT IDGETAVLTL
     EVAQHIGDNT IRAISMQQTD GLVRGAPVRD TGAPISVPVG NATKGHVFNV LGNPLDVDKV
     DAETYWPIHR SAPAFDQLES KTEMFTTGIK VIDLLAPYVR GGKIGLMGGA GVGKTVIIQE
     MIRRVAKEFG GVSVFAGVGE RTREGNDLFL EMTEAGVIED TALVFGQMDE PPGTRLRVAL
     GALTMAEYFR DVQKQDVLLF IDNIFRFTQA GSEVSTLLGR MPSAVGYQPT LADEMGALQE
     RITSTRGHSI TSLQAIYVPA DDLTDPAPAT TFTHLDANTV LDRAISDLGI YPAVSPLDSN
     SRILDARYIG QEHYDTAREV QRILQRYKDL QDIIAILGID ELSEEDKILV NRARRIQRFL
     SQPFFVAEQF TGIPGKFVPL DETIDSFRRL TQGDYDHLPE QAFFMCGGIE DAEKNAENL
//

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