CLPC_TRICV
ID CLPC_TRICV Reviewed; 885 AA.
AC P49574;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA homolog;
GN Name=clpC;
OS Trieres chinensis (Marine centric diatom) (Odontella sinensis).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae;
OC Biddulphiophycidae; Eupodiscales; Parodontellaceae; Trieres.
OX NCBI_TaxID=1514140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kowallik K.V., Stoebe B., Schaffran I., Kroth-Pancic P., Freier U.;
RT "The chloroplast genome of a chlorophyll a+c-containing alga, Odontella
RT sinensis.";
RL Plant Mol. Biol. Rep. 13:336-342(1995).
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; Z67753; CAA91619.1; -; Genomic_DNA.
DR PIR; S78246; S78246.
DR AlphaFoldDB; P49574; -.
DR SMR; P49574; -.
DR PRIDE; P49574; -.
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 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.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Plastid; Repeat.
FT CHAIN 1..885
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpA
FT homolog"
FT /id="PRO_0000191218"
FT DOMAIN 2..145
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 5..70
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 80..145
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 864..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 560..567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 885 AA; 99918 MW; 8F5BE76B5A65380B CRC64;
MFEKFTEGAI KVIMLSQEEA RRMGHNFVGT EQLLLGIIGQ RHGIGARALK KQKVTLKKAR
REIELYIGRG TGFVASEIPF TPRAKRVLEM AVHEGKDLGQ NFVGTEHILL ALISESDGVA
MRTLDKLGVN IPKLRNLILM YIEENQEEIL RPLTQAEKFL LEREKKGSST PTLDEYSENI
SKEAVDGKLD PVIGRDKEIH EVIKVLARRR KNNPVLIGEP GVGKTAVAEG LAQLIIAEKA
PDFLDGNLLM ALDLGSILAG TKYRGEFEER IKRIVEEVQN DSAIILVIDE IHTLVGAGAA
EGAVDAANIL KPALARGKFR CIGATTIDEY RKYIERDPAL ERRFQPVHVK EPTVGVTIEI
LLGLRSKFEE HHTLSYHDKA VEQAAILADK FIADRFLPDK AIDVLDEAGS RVRLENRRLP
RGMKRLLKEL QDTLRDKEES IKEHDFDIAK QLVDHEMEVR THIRIMKQSI LTNETLGLAR
KEIDTVLEGD VAEVIAGWTG IPVNKISDSE SKRLLTMEET LHERLIGQHH AIVSVSKAIR
RARVGLRNPD RPIASFIFAG PTGVGKTELT KALSEYMFGN EDSMIRLDMS EYMEKHTVAK
LIGSPPGYVG YNEGGQLTEA VQTKPYSVVL LDEVEKAHPD VFNLLLQILD DGRLTDSKGR
TIDFRNTMII MTTNLGAKII EKESGIKPKT KQDKPAFRID ESGCLGWEPT PEPIKDSALF
EKVTELVNEE LKEFFRPEFL NRIDEIIVFN HLTKYDIWEI CGLMVKQLQK RLEEKELTLE
VDVSVRNLLT EEGYDPVYGA RPLRRAVMRL LEDTLAQQCL SKPLYPGTIL RVSRVKEEGT
LASYTNDVKV EIDYRRVDPR LLEQAEEKKE QNQEETKQNI LKTDA