ID   CLPC_PEA                Reviewed;         922 AA.
AC   P35100;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Chaperone protein ClpC, chloroplastic;
DE   AltName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC homolog;
DE   AltName: Full=Casein lytic proteinase C;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Little Marvel;
RX   PubMed=8443344; DOI=10.1007/bf00028809;
RA   Moore T., Keegstra K.;
RT   "Characterization of a cDNA clone encoding a chloroplast-targeted Clp
RT   homologue.";
RL   Plant Mol. Biol. 21:525-537(1993).
RN   [2]
RP   FUNCTION, AND CLASSIFICATION.
RX   PubMed=1735703; DOI=10.1128/jb.174.4.1081-1085.1992;
RA   Squires C., Squires C.L.;
RT   "The Clp proteins: proteolysis regulators or molecular chaperones?";
RL   J. Bacteriol. 174:1081-1085(1992).
CC   -!- FUNCTION: Molecular chaperone that may interact with a ClpP-like
CC       protease involved in degradation of denatured proteins in the
CC       chloroplast. {ECO:0000269|PubMed:1735703}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L09547; AAA33680.1; -; mRNA.
DR   PIR; S31164; S31164.
DR   AlphaFoldDB; P35100; -.
DR   SMR; P35100; -.
DR   DIP; DIP-729N; -.
DR   IntAct; P35100; 2.
DR   MEROPS; X20.001; -.
DR   PRIDE; P35100; -.
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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Plastid; Repeat;
KW   Transit peptide.
FT   TRANSIT         1..72
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           73..922
FT                   /note="Chaperone protein ClpC, chloroplastic"
FT                   /id="PRO_0000005504"
FT   DOMAIN          92..234
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   DOMAIN          509..544
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT   REGION          95..160
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          170..234
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          255..502
FT                   /note="I"
FT   REGION          569..760
FT                   /note="II"
FT   BINDING         300..307
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         643..650
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   922 AA;  102711 MW;  1CA4C1BA7D453DFE CRC64;
     MARVLAQSLS VPGLVAGHKD SQHKGSGKSK RSVKTMCALR TSGLRMSGFS GLRTFNHLNT
     MMRPGLDFHS KVSKAVSSRR ARAKRFIPRA MFERFTEKAI KVIMLAQEEA RRLGHNFVGT
     EQILLGLIGE GTGIAAKVLK SMGINLKDAR VEVEKIIGRG SGFVAVEIPF TPRAKRVLEL
     SQEEARQLGH NYIGSEHLLL GLLREGEGVA ARVLENLGAD PTNIRTQVIR MVGESADSVT
     ATVGSGSSNN KTPTLEEYGT NLTKLAEEGK LDPVVGRQPQ IERVTQILGR RTKNNPCLIG
     EPGVGKTAIA EGLAQRIANG DVPETIEGKK VITLDMGLLV AGTKYRGEFE ERLKKLMEEI
     KQSDDIILFI DEVHTLIGAG AAEGAIDAAN ILKPALARGE LQCIGATTLD EYRKHIEKDP
     DLERRFQPVK VPEPTVDETI QILKGLRERY EIHHKLRYTD EALIAAAQLS YQYISDRFLP
     DKAIDLVDEA GSRVRLQHAQ LPEEAKELDK EVRKIVKEKE EYVRNQDFEK AGELRDKEMD
     LKAQISALIE KGKEMSKAET ETADEGPIVT EVDIQHIVSS WTGIPVDKVS ADESDRLLKM
     EDTLHKRIIG QDEAVQAISR AIRRARVGLK NPNRPIASFI FSGPTGVGKS ELAKALAAYY
     FGSEEAMIRL DMSEFMERHT VSKLIGSPPG YVGYTEGGQL TEAVRRRPYT VVLFDEIEKA
     HPDVFNMMLQ ILEDGRLTDS KGRTVDFKNT LLIMTSNVGS SVIEKGGRRI GFDLDYDEKD
     SSYNRIKSLV TEELKQYFRP EFLNRLDEMI VFRQLTKLEV KEIADIMLKE VFQRLKTKEI
     ELQVTERFRD RVVDEGYNPS YGARPLRRAI MRLLEDSMAE KMLAREIKEG DSVIVDVDSD
     GKVIVLNGSS GTPESLPEAL SI