ATPF2_CHLRE
ID ATPF2_CHLRE Reviewed; 209 AA.
AC A8J785; Q9S882;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=ATP synthase subunit b', chloroplastic {ECO:0000303|PubMed:8543042};
DE AltName: Full=ATP synthase F(0) sector subunit b';
DE AltName: Full=ATPase subunit II;
DE Flags: Precursor;
GN Name=ATPF2 {ECO:0000305}; Synonyms=atpG {ECO:0000303|PubMed:8543042};
GN ORFNames=CHLREDRAFT_206190;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503, and cw92;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [2]
RP PROTEIN SEQUENCE OF 63-82, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=cw15;
RX PubMed=8543042; DOI=10.1016/0014-5793(95)01332-6;
RA Fiedler H.R., Schmid R., Leu S., Shavit N., Strotmann H.;
RT "Isolation of CF0CF1 from Chlamydomonas reinhardtii cw15 and the N-terminal
RT amino acid sequences of the CF0CF1 subunits.";
RL FEBS Lett. 377:163-166(1995).
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.
CC {ECO:0000269|PubMed:8543042}.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged
CC and duplicated form of b found in plants and photosynthetic bacteria.
CC {ECO:0000305}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main
CC subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC form an alternating ring which encloses part of the gamma chain. F(1)
CC is attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta, b and b'
CC chains. {ECO:0000269|PubMed:8543042}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:8543042}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CC CF(1)CF(0). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000305}.
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; DS496140; EDP00272.1; -; Genomic_DNA.
DR RefSeq; XP_001697332.1; XM_001697280.1.
DR AlphaFoldDB; A8J785; -.
DR SMR; A8J785; -.
DR STRING; 3055.EDP00272; -.
DR PaxDb; A8J785; -.
DR ProMEX; A8J785; -.
DR EnsemblPlants; PNW76927; PNW76927; CHLRE_11g481450v5.
DR GeneID; 5722943; -.
DR Gramene; PNW76927; PNW76927; CHLRE_11g481450v5.
DR KEGG; cre:CHLRE_11g481450v5; -.
DR eggNOG; ENOG502RH8G; Eukaryota.
DR HOGENOM; CLU_079215_0_2_1; -.
DR InParanoid; A8J785; -.
DR OMA; PLMAIQF; -.
DR OrthoDB; 1604952at2759; -.
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:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR HAMAP; MF_01399; ATP_synth_bprime; 1.
DR InterPro; IPR034679; ATP_synth_b.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR Pfam; PF00430; ATP-synt_B; 1.
PE 1: Evidence at protein level;
KW ATP-binding; CF(0); Chloroplast; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Plastid; Thylakoid; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:8543042"
FT CHAIN 63..209
FT /note="ATP synthase subunit b', chloroplastic"
FT /id="PRO_0000388330"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 72
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="F -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 22479 MW; 46C4CD72D2F31E08 CRC64;
MASLLARPQQ AVVRAAKPAA ARPLRLVVRA SAQKPQQQLA QLAKPALSAI VANALMAMPA
AAEAGKIFDF NLTLPVMAGE FLLLMVFLEK TWFTPVGKVL DERDNLIRSK LGSVKDNTGD
VDKLVLEAET ILKSARSDVS AMINTKKAAK QSELDKTYNE AKAKITAEVE SSIAGLEQES
ASMLKSLDAQ VDKISAEVLK RVLPEGVRV
