ID   CLPAA_SOLLC             Reviewed;         926 AA.
AC   P31541;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA homolog CD4A, chloroplastic;
DE   Flags: Precursor;
GN   Name=CD4A;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2185473; DOI=10.1073/pnas.87.9.3513;
RA   Gottesman S., Squires C., Pichersky E., Carrington M., Hobbs M.,
RA   Mattick J.S., Dalrymple B., Kuramitsu H., Shiroza T., Foster T.,
RA   Clark W.P., Ross B., Squires C.L., Maurizi M.R.;
RT   "Conservation of the regulatory subunit for the Clp ATP-dependent protease
RT   in prokaryotes and eukaryotes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:3513-3517(1990).
CC   -!- FUNCTION: May interact with a ClpP-like protease involved in
CC       degradation of denatured proteins in the chloroplast.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M32603; AAA34160.1; -; Genomic_DNA.
DR   PIR; A35905; A35905.
DR   AlphaFoldDB; P31541; -.
DR   SMR; P31541; -.
DR   STRING; 4081.Solyc03g118340.2.1; -.
DR   MEROPS; X20.001; -.
DR   PaxDb; P31541; -.
DR   PRIDE; P31541; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   InParanoid; P31541; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P31541; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Plastid;
KW   Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..926
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpA
FT                   homolog CD4A, chloroplastic"
FT                   /id="PRO_0000005502"
FT   DOMAIN          94..236
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   DOMAIN          511..546
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT   REGION          97..162
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          172..236
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          257..504
FT                   /note="I"
FT   REGION          572..763
FT                   /note="II"
FT   BINDING         302..309
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         646..653
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   926 AA;  102557 MW;  30FA31F892E0916C CRC64;
     MMARALVQST NILPSVAGER AGQFNGSRKD QRTVRMLCNV KCCSSRLNNF AGLRGCNALD
     TLLVKSGETL HSKVAAATFV RRPRGCRFVP KAMFERFTEK AIKVIMLAQE EARRLGHNFV
     GTEQILLGLI GEGTGIAAKV LKSMGINLKD ARVEVEKIIG RGSGFIAVEI PFTPRAKRVL
     ELSLEEARQL GHNYIGSEHL LLGLLREGEG VAARVLENLG ADPTNIRTQV IRMVGESSEA
     VGASVGGGTS GLKMPTLEEY GTNLTKLAEE GKLDPVVGRQ AQIERVTQIL GRRTKNNPCL
     IGEPGVGKTA IAEGLAQRIA NGDVPETIEG KKVITLDMGL LVAGTKYRGE FEERLKKLME
     EIKQSDEIIL FIDEVHTLIG AGAAEGAIDA ANILKPALAR GELQCIGATT LDEYRKHIEK
     DPALERRFQP VKVPEPSVDE TIQILKGLRE RYEIHHKLHY TDEAIEAAAK LSHQYISDRF
     LPDKAIDLID EAGSRVRLRH AQLPEEAREL EKELRQITKE KNEAVRGQDF EKAGELRDRE
     MDLKAQISAL IDKNKEKSKA ESEAGDAAGP IVTEADIQHI VSSWTGIPVE KVSTDESDRL
     LKMEETLHTR VIGQDEAVKA ISRAIRRARV GLKNPNRPIA SFIFSGPTGV GKSELAKSLA
     TYYFGSEEAM IRLDMSEFME RHTVSKLIGS PPGYVGYTEG GQLTEAVRRR PYTVVLFDEI
     EKAHPDVFNM MLQILEDGRL TDSKGRTVDF KNTLLIMTSN VGSSVIEKGG RRIGFDLDFD
     EKDSSYNRIK SLVTEELKQY FRPEFLNRLS EMIVFRQLTK LEVKEIADIM LKEVFVRLKN
     KEIELQVTER FRDRVVDEGY NPSYGARPLR RAIMRLLEDS MAEKMLAGEI KEGDSVIVDV
     DSDGNVTVLN GTSGAPSDSA PEPILV