(data stored in ACNUC30630 zone)

HOGENOM: CODIP1_1_PE1001

ID   CODIP1_1_PE1001                      STANDARD;      PRT;   273 AA.
AC   CODIP1_1_PE1001; Q6NHT2;
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 delta;AltName: Full=ATP synthase F(1)
DE   sector subunit delta;AltName: Full=F-type ATPase subunit delta;
DE   Short=F-ATPase subunit delta; (CODIP1_1.PE1001).
GN   Name=atpH; OrderedLocusNames=DIP1049;
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.PE1001.
CC       Corynebacterium diphtheriae NCTC 13129, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:ATPD_CORDI
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the
CC       presence of a proton or sodium gradient. F-type ATPases consist of
CC       two structural domains, F(1) containing the extramembraneous
CC       catalytic core and F(0) containing the membrane proton channel,
CC       linked together by a central stalk and a peripheral stalk. During
CC       catalysis, ATP synthesis in the catalytic domain of F(1) is
CC       coupled via a rotary mechanism of the central stalk subunits to
CC       proton translocation (By similarity).
CC   -!- FUNCTION: This protein is part of the stalk that links CF(0) to
CC       CF(1). It either transmits conformational changes from CF(0) to
CC       CF(1) or is implicated in proton conduction (By similarity).
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
CC       core - and F(0) - the membrane proton channel. F(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
CC       has three main subunits: a(1), b(2) and c(10-14). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. F(1) is attached to F(0) by a central stalk formed by
CC       the gamma and epsilon chains, while a peripheral stalk is formed
CC       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 delta chain family.
CC   -!- GENE_FAMILY: HOG000247153 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6NHT2; -.
DR   EMBL; BX248356; CAE49569.1; -; Genomic_DNA.
DR   RefSeq; NP_939410.1; NC_002935.2.
DR   GeneID; 2650815; -.
DR   GenomeReviews; BX248353_GR; DIP1049.
DR   KEGG; cdi:DIP1049; -.
DR   NMPDR; fig|257309.1.peg.1001; -.
DR   OMA; FRFGRIV; -.
DR   ProtClustDB; PRK13430; -.
DR   BioCyc; CDIP257309:DIP1049-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:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   HAMAP; MF_01416; ATP_synth_delta_bact; 1; -.
DR   InterPro; IPR000711; ATPase_F1-cplx_OSCP/dsu.
DR   InterPro; IPR020781; ATPase_F1-cplx_OSCP/dsu_CS.
DR   Gene3D; G3DSA:1.10.520.20; ATPase_F1_OSCP/d; 1.
DR   PANTHER; PTHR11910; ATPase_F1_OSCP/d; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   PRINTS; PR00125; ATPASEDELTA.
DR   TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
DR   HOGENOMDNA; CODIP1_1.PE1001; -.
KW   ATP synthesis; Cell membrane; CF(1); Complete proteome;
KW   Hydrogen ion transport; Ion transport; Membrane; Transport.
SQ   SEQUENCE   273 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MHAASREALA RVTSDLDKAL WEAKENAIAT AAHTGAELFD VVEVLDGDRA LRVAVADSAK
     SAEDRAGLVS AVFAGKVSPA TLEVLVTSAR ELWSNPREFR DGLVTLGRRA LLRSAEGQGQ
     LGQVEDELFR LSRILDKEPE LTLLLDDRST DGAKKRELLA KVLYGKVTAV TEALALQVIG
     RRESNAIDDI DALSKEAAAL QGHSVAHVVS AGRLNDEQNQ ALAQKLERIY GRAMSIHSEV
     DPSLLGGLVI RVGDEVIDGS TSGKLERLRA NLA
//

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