ID   ATPG_VIGUN              Reviewed;         118 AA.
AC   Q2LGZ2;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=ATP synthase subunit gamma, chloroplastic;
DE   AltName: Full=F-ATPase gamma subunit;
DE   Contains:
DE     RecName: Full=Inceptin;
DE   Flags: Fragment;
OS   Vigna unguiculata (Cowpea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-39, AND FUNCTION OF
RP   INCEPTIN.
RC   STRAIN=cv. California Blackeye no.5;
RX   PubMed=16720701; DOI=10.1073/pnas.0602328103;
RA   Schmelz E.A., Carroll M.J., Leclere S., Phipps S.M., Meredith J.,
RA   Chourey P.S., Alborn H.T., Teal P.E.;
RT   "Fragments of ATP synthase mediate plant perception of insect attack.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:8894-8899(2006).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The gamma chain is believed to be important in
CC       regulating ATPase activity and the flow of protons through the CF(0)
CC       complex. {ECO:0000269|PubMed:16720701}.
CC   -!- FUNCTION: Inceptin is a proteolytic fragment produced by insect larvae
CC       that previously ingested the protein. This peptide mediate plant
CC       perception of herbivory through the induction of volatile,
CC       phenylpropanoid and protease inhibitor defenses such as ethylene,
CC       jasmonic acid and salicylic acid for example.
CC       {ECO:0000269|PubMed:16720701}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR   EMBL; DQ312300; ABC42340.1; -; mRNA.
DR   AlphaFoldDB; Q2LGZ2; -.
DR   SMR; Q2LGZ2; -.
DR   PRIDE; Q2LGZ2; -.
DR   GO; GO:0009535; C:chloroplast thylakoid 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:InterPro.
DR   InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR   InterPro; IPR000131; ATP_synth_F1_gsu.
DR   PANTHER; PTHR11693; PTHR11693; 1.
DR   Pfam; PF00231; ATP-synt; 1.
DR   SUPFAM; SSF52943; SSF52943; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Chloroplast; Direct protein sequencing;
KW   Disulfide bond; Hydrogen ion transport; Ion transport; Membrane; Plastid;
KW   Thylakoid; Transport.
FT   CHAIN           <1..>118
FT                   /note="ATP synthase subunit gamma, chloroplastic"
FT                   /id="PRO_0000245320"
FT   PEPTIDE         29..39
FT                   /note="Inceptin"
FT                   /id="PRO_0000245321"
FT   DISULFID        30..36
FT   NON_TER         1
FT   NON_TER         118
SQ   SEQUENCE   118 AA;  13024 MW;  4BA1985F83DD541E CRC64;
     DPLYTKFVSL VKSDPVIHTL LPLSPKGEIC DINGVCVDAA EDEFFRLTTK EGKLTVERDV
     VRTKTTDYSP ILQFEQDPVQ ILDALLPLYL NSQILRALQE SLASELAARM SAMSNAAA