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Database: UniProt
Entry: P49574
LinkDB: P49574
Original site: P49574 
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-MAY-2023, entry version 99.
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   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   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
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   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF155; CLP PROTEASE ATP-BINDING SUBUNIT; 1.
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; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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
//
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