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Entry: A0A0D1XN43_ANEMI
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ID   A0A0D1XN43_ANEMI        Unreviewed;       179 AA.
AC   A0A0D1XN43;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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   ORFNames=AF333_02400 {ECO:0000313|EMBL:KON94510.1}, SAMN04487909_10449
GN   {ECO:0000313|EMBL:SDI44754.1};
OS   Aneurinibacillus migulanus (Bacillus migulanus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=47500 {ECO:0000313|EMBL:KON94510.1, ECO:0000313|Proteomes:UP000037269};
RN   [1] {ECO:0000313|EMBL:KON94510.1, ECO:0000313|Proteomes:UP000037269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2895 {ECO:0000313|EMBL:KON94510.1,
RC   ECO:0000313|Proteomes:UP000037269};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-14205 dsm 2895.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SDI44754.1, ECO:0000313|Proteomes:UP000182836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2895 {ECO:0000313|EMBL:SDI44754.1,
RC   ECO:0000313|Proteomes:UP000182836};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-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; LGUG01000004; KON94510.1; -; Genomic_DNA.
DR   EMBL; FNED01000004; SDI44754.1; -; Genomic_DNA.
DR   RefSeq; WP_043067559.1; NZ_LIXL01000244.1.
DR   STRING; 47500.AF333_02400; -.
DR   PATRIC; fig|47500.12.peg.6035; -.
DR   OrthoDB; 9802471at2; -.
DR   Proteomes; UP000037269; Unassembled WGS sequence.
DR   Proteomes; UP000182836; 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: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; IPR020781; ATPase_OSCP/d_CS.
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.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01416}; 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:UP000037269};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}.
SQ   SEQUENCE   179 AA;  19932 MW;  7F4C7548C2D24AE2 CRC64;
     MSAVAKRYAR ALYEVANEKQ AIDTTEVELN QITDIIKQSD ELNMLLTHPK VTAAEKKGIL
     NELFADKVSE TTLSFLNLLL ERGREDELND IAKQFTELSN EARGFADATV ITAKPLTEAE
     LEKVAEQFGQ KVNKKLRVAT KIDPSIIGGI IVRIGDRLYD GSIKGKLARF TQQIKQAQV
//
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