ID   CLPC_GUITH              Reviewed;         819 AA.
AC   O78410;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA homolog;
GN   Name=clpC;
OS   Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9929392; DOI=10.1007/pl00006462;
RA   Douglas S.E., Penny S.L.;
RT   "The plastid genome of the cryptophyte alga, Guillardia theta: complete
RT   sequence and conserved synteny groups confirm its common ancestry with red
RT   algae.";
RL   J. Mol. Evol. 48:236-244(1999).
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. {ECO:0000305}.
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DR   EMBL; AF041468; AAC35595.1; -; Genomic_DNA.
DR   RefSeq; NP_050661.1; NC_000926.1.
DR   AlphaFoldDB; O78410; -.
DR   SMR; O78410; -.
DR   PRIDE; O78410; -.
DR   GeneID; 856945; -.
DR   HOGENOM; CLU_005070_4_1_1; -.
DR   OMA; NIRRIHI; -.
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; Repeat.
FT   CHAIN           1..819
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpA
FT                   homolog"
FT                   /id="PRO_0000191217"
FT   DOMAIN          2..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   DOMAIN          416..451
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT   REGION          5..70
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          80..144
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          162..409
FT                   /note="I"
FT   REGION          472..663
FT                   /note="II"
FT   BINDING         207..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         546..553
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   819 AA;  90959 MW;  F563CFEE301A03B3 CRC64;
     MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGIAAKVLK SMGVNLKDAR
     VEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SLEEARQLGH NYIGTEHLLL GLIREGEGVA
     ARVLENLALD LTKVRTQVIR LLGDTAEVSA TNGQTKGKTP TLEEFGSNLT QKAAEGKLDP
     VIGRQKEIER VIQILGRRTK NNPILIGEPG VGKTAIAEGL AQRINNRDVP DILEDKRVVT
     LDIGLLVAGT KYRGEFEERL KKIIDEIRVA NNVILVIDEV HTLIGAGAAE GAIDAANILK
     PALARGEMQC IGATTLEEYR KHIEKDSALE RRFQPVMVGE PSVEETIEIL YGLRDRYEKH
     HKLVISDEAL SAAAKFADQY IADRFLPDKA IDLIDEAGSR VRLMNSQLPP AARELDKELR
     EILKQKDEAV RSQDFETAGQ LRDREMEIKA QIAAIAHSKK GDEENTKEVS VVTEEDIAQI
     VAAWTGIPVN KMTRSESEKL LQMEETLHGR IIGQDEAVVA VSKAIRRARV GLKNPNRPIA
     SFIFSGPTGV GKTELTKALA SYFFGSEEAM VRLDMSEYME RHTVSKLIGS PPGYVGYNEG
     GQLTESVRRR PYTVVLFDEI EKGHPDVFNL LLQILEDGRL TDSKGRTVDF KNTLLILTSN
     VGSKVIEKGG GGLGFDLSED QTESQYGRIK ALVNEELKQY FRPEFLNRLD EIIVFRQLTK
     DEVGEIAEIM LKEVFTRISE KGIQLEVTAR FKTHLINEGY NPIYGARPLR RAVMRLLEDT
     LSEEFLAEKI KEGDTAVVDV DDDGKVKVLL GEKLELVAN