(data stored in ACNUC30630 zone)

HOGENOM: CODIP1_1_PE1003

ID   CODIP1_1_PE1003                      STANDARD;      PRT;   325 AA.
AC   CODIP1_1_PE1003; Q6NHT0;
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 gamma chain;AltName: Full=ATP synthase F1
DE   sector gamma subunit;AltName: Full=F-ATPase gamma subunit;
DE   (CODIP1_1.PE1003).
GN   Name=atpG; OrderedLocusNames=DIP1051;
OS   CORYNEBACTERIUM DIPHTHERIAE NCTC 13129.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=257309;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CODIP1_1.PE1003.
CC       Corynebacterium diphtheriae NCTC 13129, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:ATPG_CORDI
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton
CC       gradient across the membrane. The gamma chain is believed to be
CC       important in regulating ATPase activity and the flow of protons
CC       through the CF(0) complex.
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, b and c.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC   -!- GENE_FAMILY: HOG000215910 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6NHT0; -.
DR   EMBL; BX248356; CAE49571.1; -; Genomic_DNA.
DR   RefSeq; NP_939412.1; NC_002935.2.
DR   ProteinModelPortal; Q6NHT0; -.
DR   GeneID; 2650817; -.
DR   GenomeReviews; BX248353_GR; DIP1051.
DR   KEGG; cdi:DIP1051; -.
DR   NMPDR; fig|257309.1.peg.1003; -.
DR   OMA; AGNLIND; -.
DR   PhylomeDB; Q6NHT0; -.
DR   ProtClustDB; PRK05621; -.
DR   BioCyc; CDIP257309:DIP1051-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:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   HAMAP; MF_00815; ATP_synth_gamma_bact; 1; -.
DR   InterPro; IPR000131; ATPase_F1-cplx_gsu.
DR   InterPro; IPR023632; ATPase_F1_gsu_CS.
DR   InterPro; IPR023633; ATPase_F1_gsu_dom.
DR   PANTHER; PTHR11693; ATPase_F1_gamma; 1.
DR   Pfam; PF00231; ATP-synt; 1.
DR   PRINTS; PR00126; ATPASEGAMMA.
DR   SUPFAM; SSF52943; ATPase_gamma; 1.
DR   TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR   PROSITE; PS00153; ATPASE_GAMMA; 1.
DR   HOGENOMDNA; CODIP1_1.PE1003; -.
KW   ATP synthesis; Cell membrane; CF(1); Complete proteome;
KW   Hydrogen ion transport; Ion transport; Membrane; Transport.
SQ   SEQUENCE   325 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MANLRELRDR IRSVNSTKKI TKAQELIATS RITKAQARVE ASQPYATEIH KVMERLAAAS
     SLEHPMLRER EGGKRAAVLV VSSDRGMAGG YNYNVFKKAA ELEKLLEENG YEVVRYVTGN
     KGVGYYKFRG QEVAGAWTGF SQDPSWEETH DVRRHLIDGF NASSNGTARY RDGLNTDEGQ
     EIQGFDQVHV VYTEFESMLT QTARAHQLLP IEPVIETVEI PEADGILDQS GEPTPDVEFE
     PDADTLLEAL LPQYVSRSLF AMFLEAAAAE SASRRNAMKS ATDNATALVK DLSRVANQAR
     QAQITQEITE IVGGASALGD SGESD
//

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