ATPD_PHEZH
ID ATPD_PHEZH Reviewed; 184 AA.
AC B4RD44;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=ATP synthase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
GN Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416}; OrderedLocusNames=PHZ_c0234;
OS Phenylobacterium zucineum (strain HLK1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1;
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(2008).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-
CC Rule:MF_01416}.
CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CF(1).
CC It either transmits conformational changes from CF(0) to CF(1) or is
CC implicated in proton conduction. {ECO:0000255|HAMAP-Rule:MF_01416}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. F(1) is
CC attached to F(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_01416}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01416}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01416}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01416}.
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DR EMBL; CP000747; ACG76648.1; -; Genomic_DNA.
DR RefSeq; WP_012520796.1; NC_011144.1.
DR AlphaFoldDB; B4RD44; -.
DR SMR; B4RD44; -.
DR STRING; 450851.PHZ_c0234; -.
DR EnsemblBacteria; ACG76648; ACG76648; PHZ_c0234.
DR KEGG; pzu:PHZ_c0234; -.
DR eggNOG; COG0712; Bacteria.
DR HOGENOM; CLU_085114_0_1_5; -.
DR OMA; MVDNIQD; -.
DR OrthoDB; 1937493at2; -.
DR Proteomes; UP000001868; Chromosome.
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:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.520.20; -; 1.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; SSF47928; 1.
DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transport.
FT CHAIN 1..184
FT /note="ATP synthase subunit delta"
FT /id="PRO_0000371053"
SQ SEQUENCE 184 AA; 19261 MW; 67DA7315B2471A2E CRC64;
MADDSKSSNV GSRYAQALFD LASEQKEVPA VEADLKSLKA AIADSRDLRV LLASPAFGAD
DKRKGLSAIA DKAKFKPTTK KFLGLLAANG RAAALPEVIS AFERLAAEAR GAVSAEVTTA
LPLSSAQAKG LAQALRQALG KDPEITTRVD PALLGGIKVK VGSRLFDASL RSKLDSLKFA
LKRA