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Database: UniProt
Entry: A0A098Y2H9_9ACTN
LinkDB: A0A098Y2H9_9ACTN
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ID   A0A098Y2H9_9ACTN        Unreviewed;       276 AA.
AC   A0A098Y2H9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=IN07_22045 {ECO:0000313|EMBL:KGH44667.1};
OS   Modestobacter caceresii.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=1522368 {ECO:0000313|EMBL:KGH44667.1, ECO:0000313|Proteomes:UP000029713};
RN   [1] {ECO:0000313|EMBL:KGH44667.1, ECO:0000313|Proteomes:UP000029713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNN45-2b {ECO:0000313|EMBL:KGH44667.1,
RC   ECO:0000313|Proteomes:UP000029713};
RA   Bukarasam K., Bull A., Girard G., van Wezel G., Goodfellow M.;
RT   "Biosystematic studies on Modestobacter strains isolated from extreme
RT   hyper-arid desert soil and from historic building.";
RL   Submitted (JUL-2014) 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}.
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:KGH44667.1}.
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DR   EMBL; JPMX01000118; KGH44667.1; -; Genomic_DNA.
DR   RefSeq; WP_036340171.1; NZ_JPMX01000118.1.
DR   AlphaFoldDB; A0A098Y2H9; -.
DR   STRING; 1522368.IN07_22045; -.
DR   OrthoDB; 5242917at2; -.
DR   Proteomes; UP000029713; 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; IPR000711; ATPase_OSCP/dsu.
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.
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|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:UP000029713};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}.
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  29836 MW;  DC46BC85A4AF587E CRC64;
     MHASSRAAME ESRASLQEKS QGARSRNHGD VLLTLADELF AVANLLDSQP SLRRALSDAS
     VRPDDRAGLT RRLLSGQLGA DTMSVVETVA RQRWSRPRDL VEATETLGTE AALDAADARG
     ELEGVEDELF RFGRIVAGDA DLARILGDRS APREGKTALL DRLLSGRVSP VTERLVRNAL
     TSSHVHNPEN EVERLSTMAA RRRGRSVAHV TSAVPLTAVQ EQRLIDVLGR LYGRTMGLQV
     QVDPDVLGGL VVRVDDEVIN GSIAARLEAS GRRLAG
//
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