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Database: UniProt
Entry: G0AEK8_COLFT
LinkDB: G0AEK8_COLFT
Original site: G0AEK8_COLFT 
ID   G0AEK8_COLFT            Unreviewed;       179 AA.
AC   G0AEK8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
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   ECO:0000313|EMBL:AEK64216.1};
GN   OrderedLocusNames=CFU_4395 {ECO:0000313|EMBL:AEK64216.1};
OS   Collimonas fungivorans (strain Ter331).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK64216.1, ECO:0000313|Proteomes:UP000008392};
RN   [1] {ECO:0000313|EMBL:AEK64216.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK64216.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=15305924; DOI=10.1111/j.1462-2920.2004.00673.x;
RA   Leveau J.H., Gerards S., de Boer W., van Veen J.A.;
RT   "Phylogeny-function analysis of (meta)genomic libraries: screening for
RT   expression of ribosomal RNA genes by large-insert library fluorescent in
RT   situ hybridization (LIL-FISH).";
RL   Environ. Microbiol. 6:990-998(2004).
RN   [2] {ECO:0000313|EMBL:AEK64216.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK64216.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=16457898; DOI=10.1016/j.mimet.2005.12.010;
RA   Leveau J.H., Gerards S., Fritsche K., Zondag G., van Veen J.A.;
RT   "Genomic flank-sequencing of plasposon insertion sites for rapid
RT   identification of functional genes.";
RL   J. Microbiol. Methods 66:276-285(2006).
RN   [3] {ECO:0000313|EMBL:AEK64216.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK64216.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=18671744; DOI=10.1111/j.1574-6941.2008.00547.x;
RA   Fritsche K., de Boer W., Gerards S., van den Berg M., van Veen J.A.,
RA   Leveau J.H.;
RT   "Identification and characterization of genes underlying chitinolysis in
RT   Collimonas fungivorans Ter331.";
RL   FEMS Microbiol. Ecol. 66:123-135(2008).
RN   [4] {ECO:0000313|EMBL:AEK64216.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK64216.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=19638176; DOI=10.1111/j.1462-2920.2009.02010.x;
RA   Leveau J.H., Uroz S., de Boer W.;
RT   "The bacterial genus Collimonas: mycophagy, weathering and other adaptive
RT   solutions to life in oligotrophic soil environments.";
RL   Environ. Microbiol. 12:281-292(2010).
RN   [5] {ECO:0000313|EMBL:AEK64216.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK64216.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=21614084; DOI=10.1038/ismej.2011.29;
RA   Mela F., Fritsche K., de Boer W., van Veen J.A., de Graaff L.H.,
RA   van den Berg M., Leveau J.H.;
RT   "Dual transcriptional profiling of a bacterial/fungal confrontation:
RT   Collimonas fungivorans versus Aspergillus niger.";
RL   ISME J. 5:1494-1504(2011).
RN   [6] {ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392};
RA   Leveau J.H.;
RT   "Complete sequence of Collimonas fungivorans Ter331.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002745; AEK64216.1; -; Genomic_DNA.
DR   RefSeq; WP_014008366.1; NC_015856.1.
DR   AlphaFoldDB; G0AEK8; -.
DR   STRING; 1005048.CFU_4395; -.
DR   KEGG; cfu:CFU_4395; -.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_085114_3_0_4; -.
DR   Proteomes; UP000008392; 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:UP000008392};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}.
SQ   SEQUENCE   179 AA;  19035 MW;  7CB33B505C87804B CRC64;
     MAELATIARP YAEALFRVAK SQDLAAWANL VAEMGQVAVH SDVKALAHNP AVSQQQVADT
     FLALLKSPQA ANAEAKNFVA TLVDNGRLVA LPEIAEQFQV LKNAQEGAAD AEITSAFEMT
     EAQVKDLIAT LEKKFGRKLN PSVTVDNSLI GGVRVVVGDE VFDTSVRAKL QELHAALAA
//
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