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Database: UniProt
Entry: Q93MY9_LACLL
LinkDB: Q93MY9_LACLL
Original site: Q93MY9_LACLL 
ID   Q93MY9_LACLL            Unreviewed;       175 AA.
AC   Q93MY9;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 90.
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   ECO:0000313|EMBL:AAK84016.1};
GN   ORFNames=LL275_1822 {ECO:0000313|EMBL:ARD99449.1}, LLUC77_1921
GN   {ECO:0000313|EMBL:ARE09034.1};
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360 {ECO:0000313|EMBL:AAK84016.1};
RN   [1] {ECO:0000313|EMBL:AAK84016.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CHCC373 {ECO:0000313|EMBL:AAK84016.1};
RX   PubMed=12406711; DOI=10.1128/AEM.68.11.5249-5257.2002;
RA   Pedersen M.B., Koebmann B.J., Jensen P.R., Nilsson D.;
RT   "Increasing acidification of nonreplicating Lactococcus lactis deltathyA
RT   mutants by incorporating ATPase activity.";
RL   Appl. Environ. Microbiol. 68:5249-5257(2002).
RN   [2] {ECO:0000313|Proteomes:UP000191916, ECO:0000313|Proteomes:UP000192085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=275 {ECO:0000313|EMBL:ARD99449.1,
RC   ECO:0000313|Proteomes:UP000192085}, and UC77
RC   {ECO:0000313|EMBL:ARE09034.1, ECO:0000313|Proteomes:UP000191916};
RX   PubMed=28356072; DOI=.1186/s12864-017-3650-5;
RA   Kelleher P., Bottacini F., Mahony J., Kilcawley K.N., van Sinderen D.;
RT   "Comparative and functional genomics of the Lactococcus lactis taxon;
RT   insights into evolution and niche adaptation.";
RL   BMC Genomics 18:267-267(2017).
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; AF393838; AAK84016.1; -; Genomic_DNA.
DR   EMBL; CP015897; ARD99449.1; -; Genomic_DNA.
DR   EMBL; CP015906; ARE09034.1; -; Genomic_DNA.
DR   RefSeq; WP_004255262.1; NZ_WJUQ01000008.1.
DR   PATRIC; fig|1360.110.peg.1843; -.
DR   Proteomes; UP000191916; Chromosome.
DR   Proteomes; UP000192085; Chromosome.
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   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.
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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}.
SQ   SEQUENCE   175 AA;  19157 MW;  10419C6CF9EB9154 CRC64;
     MTKVNSQKYS KALLEVAQEK GQLEAILSEV SEMIQLFKED NLVAFLSSEV YSFSAKSELI
     DTLLQTSSEV MSNFLNTVRS NGRLGDLGEI LDETKNAADD MFKIADVEVV SSIALTNAQI
     EKFTAMAKAK FDLNEVTVIN TVNEKILGGF IVNSRGKIID ASLKTQLAKI AAEIL
//
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