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ATP synthase subunit c (ATP synthase F(0) sector subunit c) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein)

 A0A0C1X6H4_PSEFL        Unreviewed;        85 AA.
A0A0C1X6H4;
01-APR-2015, integrated into UniProtKB/TrEMBL.
01-APR-2015, sequence version 1.
10-OCT-2018, entry version 39.
RecName: Full=ATP synthase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
AltName: Full=F-type ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
Short=F-ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
AltName: Full=Lipid-binding protein {ECO:0000256|HAMAP-Rule:MF_01396};
Name=atpE {ECO:0000256|HAMAP-Rule:MF_01396,
ECO:0000313|EMBL:CEL26725.1};
ORFNames=AN403_3885 {ECO:0000313|EMBL:KPU60123.1},
AO356_11695 {ECO:0000313|EMBL:ALI07444.1},
AO361_03410 {ECO:0000313|EMBL:OOQ42250.1},
C0J56_30030 {ECO:0000313|EMBL:AUM72651.1},
CP336_25425 {ECO:0000313|EMBL:PCR93550.1},
DOZ69_00225 {ECO:0000313|EMBL:RAI69609.1},
DOZ80_12995 {ECO:0000313|EMBL:RAI70493.1},
QS95_01520 {ECO:0000313|EMBL:KIF64102.1},
RL74_00100 {ECO:0000313|EMBL:KIQ61454.1},
SRM1_00046 {ECO:0000313|EMBL:CEL26725.1},
TK06_21090 {ECO:0000313|EMBL:AMZ73481.1},
UG46_00575 {ECO:0000313|EMBL:KJH88528.1},
VC35_07095 {ECO:0000313|EMBL:KJZ47737.1};
Pseudomonas fluorescens.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=294 {ECO:0000313|EMBL:KIF64102.1, ECO:0000313|Proteomes:UP000031587};
[1] {ECO:0000313|EMBL:KIF64102.1, ECO:0000313|Proteomes:UP000031587}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SF4c {ECO:0000313|EMBL:KIF64102.1,
ECO:0000313|Proteomes:UP000031587};
Underwood G.E., Ly L.K., Bitzer A.S., Godino A., Bucci V., Fischer S.,
Silby M.W.;
"Draft genome sequence of Pseudomonas fluorescens strains SF4c
SF39a.";
Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:CEL26725.1}
NUCLEOTIDE SEQUENCE.
STRAIN=SRM1 {ECO:0000313|EMBL:CEL26725.1};
Lo Raquel;
Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:CEL26725.1, ECO:0000313|Proteomes:UP000043897}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SRM1 {ECO:0000313|EMBL:CEL26725.1};
Lo R., Stanton-Cook M.J., Beatson S.A., Turner M.S., Bansal N.;
"Draft genome sequence of Pseudomonas fluorescens SRM1, an isolate
from spoiled raw milk.";
Genome Announc. 3:e00138-e00138(2015).
[4] {ECO:0000313|EMBL:KIQ61454.1, ECO:0000313|Proteomes:UP000032101}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UM270 {ECO:0000313|EMBL:KIQ61454.1,
ECO:0000313|Proteomes:UP000032101};
Hernandez-Salmeron J.E., Santoyo G., Moreno-Hagelsieb G.,
Hernandez-Leon R.;
"Draft Genome Sequence of the Biocontrol and Plant Growth-Promoting
Rhizobacteria (PGPR) Pseudomonas fluorescens UM270.";
Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:KJH88528.1, ECO:0000313|Proteomes:UP000032488}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NT0133 {ECO:0000313|EMBL:KJH88528.1,
ECO:0000313|Proteomes:UP000032488};
Tovi N., Frenk S., Hadar Y., Minz D.;
"Draft genome sequence of Pseudomonas fluorescens NT0133 isolated from
wheat (Triticum turgidum) rhizosphere.";
Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:KJZ47737.1, ECO:0000313|Proteomes:UP000033588}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C8 {ECO:0000313|EMBL:KJZ47737.1,
ECO:0000313|Proteomes:UP000033588};
Qin Y.;
"Comparative genomics of Pseudomonas insights into diversity of traits
involved in vanlence and defense.";
Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000313|Proteomes:UP000059425}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FW300-N2C3 {ECO:0000313|Proteomes:UP000059425};
Ray J., Melnyk R., Deutschbauer A.;
"Whole genome sequence of Pseudomonas fluorescens FW300-N2C3.";
Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000313|Proteomes:UP000220145}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GW456-L13 {ECO:0000313|Proteomes:UP000220145};
Ray J., Melnyk R., Deutschbauer A.;
"Whole genome sequence of Pseudomonas fluorescens GW456-L13.";
Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
[9] {ECO:0000313|EMBL:KPU60123.1, ECO:0000313|Proteomes:UP000050349}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=S613 {ECO:0000313|EMBL:KPU60123.1,
ECO:0000313|Proteomes:UP000050349};
Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
[10] {ECO:0000313|Proteomes:UP000076083}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FW300-N2E2 {ECO:0000313|Proteomes:UP000076083};
Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K.,
Barbian K., Babar A., Rosenke K.;
Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
[11] {ECO:0000313|EMBL:PCR93550.1, ECO:0000313|Proteomes:UP000217993}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CH267 {ECO:0000313|EMBL:PCR93550.1,
ECO:0000313|Proteomes:UP000217993};
Haney C.H., Wiesmann C.L., Shapiro L.R., O'Sullivan L.R.,
Khorasani S., Melnyk R.A., Xiao L., Bush J., Carrillo J., Pierce N.E.,
Ausubel F.M.;
"Rhizosphere-associated Pseudomonas modulate jasmonic acid/salicylic
acid antagonism to induce systemic resistance to herbivores at the
cost of susceptibility to pathogens.";
Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
[12] {ECO:0000313|EMBL:AUM72651.1, ECO:0000313|Proteomes:UP000235160}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=2P24 {ECO:0000313|EMBL:AUM72651.1,
ECO:0000313|Proteomes:UP000235160};
Wei H.-L., Yan Q., Wu X.-G., Tian T., Zhang W., Lu C.-H., Li X.,
Zhang L.-Q.;
"The genome sequence of plant growth-promoting Pseudomonas fluorescens
2P24.";
Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
[13] {ECO:0000313|EMBL:ALI07444.1}
NUCLEOTIDE SEQUENCE.
STRAIN=FW300-N2C3 {ECO:0000313|EMBL:ALI07444.1},
FW300-N2E2 {ECO:0000313|EMBL:AMZ73481.1}, and
GW456-L13 {ECO:0000313|EMBL:OOQ42250.1};
PubMed=29769716; DOI=.1038/s41586-018-0124-0;
Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K.,
Esquivel Z., Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E.,
Wall J.D., Visel A., Bristow J., Blow M.J., Arkin A.P.,
Deutschbauer A.M.;
"Mutant phenotypes for thousands of bacterial genes of unknown
function.";
Nature 557:503-509(2018).
[14] {ECO:0000313|EMBL:RAI69609.1, ECO:0000313|Proteomes:UP000249106}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HPB {ECO:0000313|EMBL:RAI69609.1,
ECO:0000313|Proteomes:UP000249106};
Koziol L.J., Ramsey A.R., Sevigny J.L.;
"Genome Sequencing of Pseudomonas species.";
Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
[15] {ECO:0000313|EMBL:RAI70493.1, ECO:0000313|Proteomes:UP000249493}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LY3 {ECO:0000313|EMBL:RAI70493.1,
ECO:0000313|Proteomes:UP000249493};
Zhirakovskaya E.;
Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the
presence of a proton or sodium gradient. F-type ATPases consist of
two structural domains, F(1) containing the extramembraneous
catalytic core and F(0) containing the membrane proton channel,
linked together by a central stalk and a peripheral stalk. During
catalysis, ATP synthesis in the catalytic domain of F(1) is
coupled via a rotary mechanism of the central stalk subunits to
proton translocation. {ECO:0000256|HAMAP-Rule:MF_01396}.
-!- FUNCTION: Key component of the F(0) channel; it plays a direct
role in translocation across the membrane. A homomeric c-ring of
between 10-14 subunits forms the central stalk rotor element with
the F(1) delta and epsilon subunits. {ECO:0000256|HAMAP-
Rule:MF_01396}.
-!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
core - and F(0) - the membrane proton channel. F(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
has three main subunits: a(1), b(2) and c(10-14). The alpha and
beta chains form an alternating ring which encloses part of the
gamma chain. F(1) is attached to F(0) by a central stalk formed by
the gamma and epsilon chains, while a peripheral stalk is formed
by the delta and b chains. {ECO:0000256|SAAS:SAAS00987430}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
Rule:MF_01396}; Multi-pass membrane protein {ECO:0000256|HAMAP-
Rule:MF_01396}.
-!- SIMILARITY: Belongs to the ATPase C chain family.
{ECO:0000256|HAMAP-Rule:MF_01396}.
-----------------------------------------------------------------------
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EMBL; CP012831; ALI07444.1; -; Genomic_DNA.
EMBL; CP015225; AMZ73481.1; -; Genomic_DNA.
EMBL; CP025542; AUM72651.1; -; Genomic_DNA.
EMBL; CDMF01000001; CEL26725.1; -; Genomic_DNA.
EMBL; JTGH01000002; KIF64102.1; -; Genomic_DNA.
EMBL; JXNZ01000001; KIQ61454.1; -; Genomic_DNA.
EMBL; JYHW01000001; KJH88528.1; -; Genomic_DNA.
EMBL; LACC01000011; KJZ47737.1; -; Genomic_DNA.
EMBL; LJXB01000071; KPU60123.1; -; Genomic_DNA.
EMBL; LKBJ01000002; OOQ42250.1; -; Genomic_DNA.
EMBL; NXNJ01000018; PCR93550.1; -; Genomic_DNA.
EMBL; QLIO01000001; RAI69609.1; -; Genomic_DNA.
EMBL; QLIN01000004; RAI70493.1; -; Genomic_DNA.
RefSeq; WP_003097235.1; NZ_QLIO01000001.1.
EnsemblBacteria; ALI07444; ALI07444; AO356_11695.
EnsemblBacteria; AMZ73481; AMZ73481; TK06_21090.
EnsemblBacteria; CEL26725; CEL26725; SRM1_00046.
EnsemblBacteria; KIF64102; KIF64102; QS95_01520.
EnsemblBacteria; KIF64549; KIF64549; NX10_03255.
EnsemblBacteria; KIP94515; KIP94515; RU10_09225.
EnsemblBacteria; KIQ61454; KIQ61454; RL74_00100.
EnsemblBacteria; KJH88528; KJH88528; UG46_00575.
EnsemblBacteria; KJZ47737; KJZ47737; VC35_07095.
EnsemblBacteria; KPU60123; KPU60123; AN403_3885.
GeneID; 34132022; -.
PATRIC; fig|294.124.peg.21; -.
eggNOG; ENOG4105KY6; Bacteria.
eggNOG; COG0636; LUCA.
Proteomes; UP000031587; Unassembled WGS sequence.
Proteomes; UP000032101; Unassembled WGS sequence.
Proteomes; UP000032488; Unassembled WGS sequence.
Proteomes; UP000033588; Unassembled WGS sequence.
Proteomes; UP000043897; Unassembled WGS sequence.
Proteomes; UP000050349; Unassembled WGS sequence.
Proteomes; UP000059425; Chromosome.
Proteomes; UP000076083; Chromosome.
Proteomes; UP000217993; Unassembled WGS sequence.
Proteomes; UP000220145; Unassembled WGS sequence.
Proteomes; UP000235160; Chromosome.
Proteomes; UP000249106; Unassembled WGS sequence.
Proteomes; UP000249493; Unassembled WGS sequence.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule.
Gene3D; 1.20.20.10; -; 1.
HAMAP; MF_01396; ATP_synth_c_bact; 1.
InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
InterPro; IPR000454; ATP_synth_F0_csu.
InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
InterPro; IPR038662; ATP_synth_F0_csu_sf.
InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
InterPro; IPR035921; F/V-ATP_Csub_sf.
PANTHER; PTHR10031; PTHR10031; 1.
Pfam; PF00137; ATP-synt_C; 1.
PRINTS; PR00124; ATPASEC.
SUPFAM; SSF81333; SSF81333; 1.
TIGRFAMs; TIGR01260; ATP_synt_c; 1.
PROSITE; PS00605; ATPASE_C; 1.
3: Inferred from homology;
ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01396};
Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396,
ECO:0000256|SAAS:SAAS00987420};
CF(0) {ECO:0000256|HAMAP-Rule:MF_01396};
Complete proteome {ECO:0000313|Proteomes:UP000031587,
ECO:0000313|Proteomes:UP000032101, ECO:0000313|Proteomes:UP000032488,
ECO:0000313|Proteomes:UP000033588};
Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
Hydrolase {ECO:0000313|EMBL:KPU60123.1};
Ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
Lipid-binding {ECO:0000256|HAMAP-Rule:MF_01396};
Membrane {ECO:0000256|HAMAP-Rule:MF_01396,
ECO:0000256|SAAS:SAAS00987420};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_01396};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01396};
Transport {ECO:0000256|HAMAP-Rule:MF_01396}.
TRANSMEM 6 31 Helical. {ECO:0000256|HAMAP-
Rule:MF_01396}.
TRANSMEM 52 76 Helical. {ECO:0000256|HAMAP-
Rule:MF_01396}.
DOMAIN 10 72 ATP-synt_C. {ECO:0000259|Pfam:PF00137}.
SITE 60 60 Reversibly protonated during proton
transport. {ECO:0000256|HAMAP-
Rule:MF_01396}.
SEQUENCE 85 AA; 8608 MW; B01B0FBEF0305B22 CRC64;
METVVGLTAI AVALLIGLGA LGTAIGFGLL GGKFLEGAAR QPEMVPMLQV KMFIVAGLLD
AVTMIGVGIA LFFTFANPFV GQIAG


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