ID A0A0T2KRP0_9MICO Unreviewed; 86 AA.
AC A0A0T2KRP0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=ATP synthase F0F1 subunit epsilon {ECO:0000313|EMBL:KRA22352.1};
GN ORFNames=ASD65_17895 {ECO:0000313|EMBL:KRA22352.1};
OS Microbacterium sp. Root61.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA22352.1, ECO:0000313|Proteomes:UP000051216};
RN [1] {ECO:0000313|EMBL:KRA22352.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA22352.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA22352.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA22352.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC {ECO:0000256|ARBA:ARBA00005712}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRA22352.1}.
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DR EMBL; LMGU01000002; KRA22352.1; -; Genomic_DNA.
DR RefSeq; WP_056225919.1; NZ_LMGU01000002.1.
DR AlphaFoldDB; A0A0T2KRP0; -.
DR STRING; 1736570.ASD65_17895; -.
DR OrthoDB; 9791445at2; -.
DR Proteomes; UP000051216; Unassembled WGS sequence.
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:InterPro.
DR CDD; cd12152; F1-ATPase_delta; 1.
DR Gene3D; 2.60.15.10; F0F1 ATP synthase delta/epsilon subunit, N-terminal; 1.
DR InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR Pfam; PF02823; ATP-synt_DE_N; 1.
DR SUPFAM; SSF51344; Epsilon subunit of F1F0-ATP synthase N-terminal domain; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023196};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000051216};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 3..82
FT /note="ATP synthase F1 complex delta/epsilon subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02823"
SQ SEQUENCE 86 AA; 8791 MW; 0F573B17ADCAD54D CRC64;
MALHVSLVSA DAEVWSGEAS LVVAKTVEGE IGFMAGHEPV LAILAEGQVR ITGTDGVKII
ANAQDGFLSM ENDDLTIVAG NAALIA
//
