ATPI_ANTSP
ID ATPI_ANTSP Reviewed; 248 AA.
AC Q02847;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=ATP synthase subunit a, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=F-ATPase subunit IV {ECO:0000255|HAMAP-Rule:MF_01393};
GN Name=atpI {ECO:0000255|HAMAP-Rule:MF_01393};
OS Antithamnion sp. (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC Ceramiaceae; Antithamnion; unclassified Antithamnion.
OX NCBI_TaxID=2767;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LB 95.79;
RX PubMed=1404401; DOI=10.1016/0022-2836(92)90238-f;
RA Kostrzewa M., Zetsche K.;
RT "Large ATP synthase operon of the red alga Antithamnion sp. resembles the
RT corresponding operon in cyanobacteria.";
RL J. Mol. Biol. 227:961-970(1992).
CC -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC in the translocation of protons across the membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01393}.
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 four main
CC subunits: a, b, b' and c. {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01393}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X63382; CAA44988.1; -; Genomic_DNA.
DR PIR; S26957; S26957.
DR AlphaFoldDB; Q02847; -.
DR SMR; Q02847; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR42823; PTHR42823; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Chloroplast; Hydrogen ion transport; Ion transport;
KW Membrane; Plastid; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..248
FT /note="ATP synthase subunit a, chloroplastic"
FT /id="PRO_0000002577"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ SEQUENCE 248 AA; 27907 MW; ABA1746C2B7377DC CRC64;
MYHKEFELFY SFISVSSVEV GKHLYWTIGN YRIHGQVFIV SWLVMIVLIS LAIAGTRNLT
RTPQKFQNFM EFILEFLQDI AKNQIGEHEY RFWIPYISTI FLFILGSNWA GALIPWKLIT
LPEGELAAPT NDINTTVALA LLTSLAYFYA GLSKNGIGYF SRYIEPTPVL LPINILEDFT
KPLSLSFRLF GNVLADELVV SVFTLLVPIL IPLPVMILGL FASSIQALIF STLSAAYIGE
ALEGHGEE