ATP62_ACAM1
ID ATP62_ACAM1 Reviewed; 234 AA.
AC A8ZNS1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=ATP synthase subunit a 2 {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=ATP synthase F0 sector subunit a 2 {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=F-ATPase subunit 6 2 {ECO:0000255|HAMAP-Rule:MF_01393};
GN Name=atpB2 {ECO:0000255|HAMAP-Rule:MF_01393};
GN Synonyms=atpI2 {ECO:0000255|HAMAP-Rule:MF_01393};
GN OrderedLocusNames=AM1_D0162;
OS Acaryochloris marina (strain MBIC 11017).
OG Plasmid pREB4.
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
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DR EMBL; CP000841; ABW32657.1; -; Genomic_DNA.
DR RefSeq; WP_012167718.1; NC_009929.1.
DR AlphaFoldDB; A8ZNS1; -.
DR SMR; A8ZNS1; -.
DR EnsemblBacteria; ABW32657; ABW32657; AM1_D0162.
DR KEGG; amr:AM1_D0162; -.
DR HOGENOM; CLU_041018_2_5_3; -.
DR OMA; ITIVYYH; -.
DR OrthoDB; 867266at2; -.
DR Proteomes; UP000000268; Plasmid pREB4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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; IPR017692; Alt_ATP_synth_F0_Asu.
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; TIGR03306; altF1_A; 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); Hydrogen ion transport; Ion transport; Membrane;
KW Plasmid; Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..234
FT /note="ATP synthase subunit a 2"
FT /id="PRO_0000362215"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ SEQUENCE 234 AA; 25750 MW; FC2AD24EB6D83F90 CRC64;
MHLTPDQTIF WQWGLFSLNA TLIFTWLVMG VLVVGSWFVT RHLSASTQIS RGQNLLEVIV
LGIRDQIQEI IDQPADPYLP FIGTLFIFIA LSNLLSVIPG YQPPTGSLST TTALALCVFF
AVPLYGVQKK GVRGYLQQYL QPNPIMLPFN IIGDFSRIVA LAVRLFGNVM SGTMIVGILL
SVAPLFFPVM MQVLGLLTGV IQAYIFAILA MVFIAAASQV DQHNYQTDSE VSHG
