(data stored in SCRATCH zone)

HOGENOM: CROTZ_1_PE10

ID   CROTZ_1_PE10                         STANDARD;      PRT;   460 AA.
AC   CROTZ_1_PE10; C9Y3V7;
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   (CROTZ_1.PE10).
GN   Name=atpD; OrderedLocusNames=Ctu_00100; ORFNames=CTU_00100;
OS   CRONOBACTER TURICENSIS Z3032.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CROTZ_1.PE10.
CC       Cronobacter turicensis z3032, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C9Y3V7_CROTZ
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 inner membrane; Peripheral membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC   -!- GENE_FAMILY: HOG000009605 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C9Y3V7; -.
DR   EMBL; FN543093; CBA26614.1; -; Genomic_DNA.
DR   RefSeq; YP_003208373.1; NC_013282.2.
DR   STRING; C9Y3V7; -.
DR   GeneID; 8460093; -.
DR   GenomeReviews; FN543093_GR; Ctu_00100.
DR   KEGG; ctu:Ctu_00100; -.
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:HAMAP.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:HAMAP.
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:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:HAMAP.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1; -.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
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; 1.
DR   HOGENOMDNA; CROTZ_1.PE10; -.
KW   ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1);
KW   Complete proteome; Hydrogen ion transport; Hydrolase; Ion transport;
KW   Membrane; Nucleotide-binding; Transport.
SQ   SEQUENCE   460 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MATGKIVQVI GAVVDVEFPQ DAVPKVYDAL EVTNGNEHLV LEVQQQLGGG IVRTIAMGSS
     DGLRRGLVVT DLEHPIEVPV GKATLGRIMN VLGQPIDMKG DIGEEERWAI HRAAPSYEEL
     SSSQELLETG IKVIDLMCPF AKGGKVGLFG GAGVGKTVNM MELIRNIAIE HSGYSVFAGV
     GERTREGNDF YHEMTDSNVL DKVSLVYGQM NEPPGNRLRV ALTGLTMAEK FREEGRDVLL
     FVDNIYRYTL AGTEVSALLG RMPSAVGYQP TLAEEMGVLQ ERITSTKTGS ITSVQAVYVP
     ADDLTDPSPA TTFAHLDATV VLSRQIASLG IYPAVDPLDS TSRQLDPLVV GQEHYDTARG
     VQSILQRYQE LKDIIAILGM DELSEEDKLV VARARKIQRF LSQPFFVAEV FTGAPGKYVS
     LKDTIRGFKG IMEGEYDHLP EQAFYMVGSI DEAVEKAKKL
//

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