ID D7DPM5_METV0 Unreviewed; 178 AA.
AC D7DPM5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=ATP synthase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE AltName: Full=F-type ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE Short=F-ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
GN Name=atpH {ECO:0000256|HAMAP-Rule:MF_01416};
GN OrderedLocusNames=M301_2785 {ECO:0000313|EMBL:ADI31138.1};
OS Methylotenera versatilis (strain 301).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylotenera.
OX NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI31138.1, ECO:0000313|Proteomes:UP000000383};
RN [1] {ECO:0000313|Proteomes:UP000000383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 {ECO:0000313|Proteomes:UP000000383};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA Chistoservova L., Kalyuzhnaya M., Woyke T.;
RT "Complete sequence of Methylotenera sp. 301.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADI31138.1, ECO:0000313|Proteomes:UP000000383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 {ECO:0000313|EMBL:ADI31138.1,
RC ECO:0000313|Proteomes:UP000000383};
RX PubMed=21622745; DOI=10.1128/JB.00404-11;
RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT "Genomes of three methylotrophs from a single niche uncover genetic and
RT metabolic divergence of Methylophilaceae.";
RL J. Bacteriol. 193:3757-3764(2011).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01416}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01416}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01416}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01416}.
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DR EMBL; CP002056; ADI31138.1; -; Genomic_DNA.
DR RefSeq; WP_013149443.1; NC_014207.1.
DR AlphaFoldDB; D7DPM5; -.
DR STRING; 666681.M301_2785; -.
DR KEGG; meh:M301_2785; -.
DR eggNOG; COG0712; Bacteria.
DR HOGENOM; CLU_085114_3_0_4; -.
DR OrthoDB; 9816221at2; -.
DR Proteomes; UP000000383; 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; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 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 NCBIfam; TIGR01145; ATP_synt_delta; 1.
DR PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1.
DR PANTHER; PTHR11910:SF1; ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_01416}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01416};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01416};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_01416};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01416};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01416};
KW Reference proteome {ECO:0000313|Proteomes:UP000000383};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}.
SQ SEQUENCE 178 AA; 19105 MW; 06375FD0527D251E CRC64;
MAEISTIARP YAVAAYKLGR EQKSLAKWSE MLGFASSVAS DAQMQAYIQD PKVVSSELQA
VFLKVCGDKL NEQGQNLIKV LVDYGRMSIL PAITEAFEEL KALDEGTLDA QIIAAAKPSA
AEVKDLVKRL EAKFGKKIEA NVSVDSELIG GIKIIVGDTV IDASVKGQLQ NLAYTLSA
//
