ATPE2_PHOPR
ID ATPE2_PHOPR Reviewed; 147 AA.
AC Q6LKZ5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=ATP synthase epsilon chain 2 {ECO:0000255|HAMAP-Rule:MF_00530};
DE AltName: Full=ATP synthase F1 sector epsilon subunit 2 {ECO:0000255|HAMAP-Rule:MF_00530};
DE AltName: Full=F-ATPase epsilon subunit 2 {ECO:0000255|HAMAP-Rule:MF_00530};
GN Name=atpC2 {ECO:0000255|HAMAP-Rule:MF_00530}; OrderedLocusNames=PBPRB0137;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000255|HAMAP-Rule:MF_00530}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00530}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00530}.
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00530}.
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DR EMBL; CR378675; CAG22010.1; -; Genomic_DNA.
DR RefSeq; WP_011220234.1; NC_006371.1.
DR AlphaFoldDB; Q6LKZ5; -.
DR SMR; Q6LKZ5; -.
DR STRING; 298386.PBPRB0137; -.
DR EnsemblBacteria; CAG22010; CAG22010; PBPRB0137.
DR KEGG; ppr:PBPRB0137; -.
DR eggNOG; COG0355; Bacteria.
DR HOGENOM; CLU_084338_2_0_6; -.
DR OMA; HEDMVIA; -.
DR OrthoDB; 1696893at2; -.
DR Proteomes; UP000000593; Chromosome 2.
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:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR CDD; cd12152; F1-ATPase_delta; 1.
DR Gene3D; 2.60.15.10; -; 1.
DR HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR InterPro; IPR036794; ATP_F1_dsu/esu_C_sf.
DR InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR InterPro; IPR020547; ATP_synth_F1_dsu/esu_C.
DR InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR PANTHER; PTHR13822; PTHR13822; 1.
DR Pfam; PF00401; ATP-synt_DE; 1.
DR Pfam; PF02823; ATP-synt_DE_N; 1.
DR SUPFAM; SSF46604; SSF46604; 1.
DR SUPFAM; SSF51344; SSF51344; 1.
DR TIGRFAMs; TIGR01216; ATP_synt_epsi; 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..147
FT /note="ATP synthase epsilon chain 2"
FT /id="PRO_0000265855"
SQ SEQUENCE 147 AA; 15880 MW; D5149448374CC083 CRC64;
MAIGVTQNTF QLNIVSAEGP LFSGKAHALA ISGLDGELGI RPGHSPLLSR IKPGVAYFQT
DLKGDDEILY ISGGILEVQP SLVTVLADTA MHGKDIDEAR ANEARRAAEE NINKQGNDIN
FAQAQMDLAK AMAQLRAVEL TQKQRRR
