ATPF_CHLRE
ID ATPF_CHLRE Reviewed; 175 AA.
AC Q8HTL5; B7U1J4; Q9T2G6;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=ATP synthase subunit b, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01398, ECO:0000303|PubMed:8543042};
DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rivier C., Rahire M., Rochaix J.-D.;
RT "Chlamydomonas reinhardtii chloroplast atpF gene.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [3]
RP PROTEIN SEQUENCE OF 13-31, 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).
RN [4]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
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:0000255|HAMAP-
CC Rule:MF_01398, 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). {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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:0000255|HAMAP-Rule:MF_01398, ECO:0000269|PubMed:8543042}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01398, ECO:0000269|PubMed:8543042}; Single-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CC CF(1)CF(0).
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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DR EMBL; AY161319; AAN41265.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50141.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00955.1; -; Genomic_DNA.
DR PIR; S68393; S68393.
DR RefSeq; NP_958410.1; NC_005353.1.
DR AlphaFoldDB; Q8HTL5; -.
DR SMR; Q8HTL5; -.
DR STRING; 3055.DAA00955; -.
DR PaxDb; Q8HTL5; -.
DR PRIDE; Q8HTL5; -.
DR GeneID; 2716983; -.
DR KEGG; cre:ChreCp054; -.
DR eggNOG; ENOG502R390; Eukaryota.
DR HOGENOM; CLU_079215_8_1_1; -.
DR InParanoid; Q8HTL5; -.
DR OrthoDB; 1333093at2759; -.
DR Proteomes; UP000006906; Chloroplast.
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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01398; ATP_synth_b_bprime; 1.
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 synthesis; ATP-binding; CF(0); Chloroplast; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Plastid; Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..175
FT /note="ATP synthase subunit b, chloroplastic"
FT /id="PRO_0000082404"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT CONFLICT 13
FT /note="H -> M (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="A -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 175 AA; 20064 MW; F0FB3D5195C19B34 CRC64;
MVFLPDNILI LGHGGFGFNT NVFETNIINL AAVVGIVVSF VGKNLSSLLE DRKNTIVKNL
EEANQRAIEA EQKLTAARTQ LETAKKKAQE IREEGVLRAT QEINNVVSQH ELRLARLQEF
KQETLAFYQQ KAFKQAYLYV INKIMTRVRE RLNKGLDSTY HVVVNNFYVS RFTQF
