ID   CLPAB_SOLLC             Reviewed;         923 AA.
AC   P31542;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA homolog CD4B, chloroplastic;
DE   Flags: Precursor;
GN   Name=CD4B;
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. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M32604; AAA34161.1; -; Genomic_DNA.
DR   PIR; B35905; B35905.
DR   AlphaFoldDB; P31542; -.
DR   SMR; P31542; -.
DR   STRING; 4081.Solyc12g042060.1.1; -.
DR   MEROPS; X20.001; -.
DR   PaxDb; P31542; -.
DR   PRIDE; P31542; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   InParanoid; P31542; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P31542; 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           ?..923
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpA
FT                   homolog CD4B, chloroplastic"
FT                   /id="PRO_0000005503"
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:0000255"
FT   BINDING         643..650
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   923 AA;  102241 MW;  26E9D6CFD6974E65 CRC64;
     MARALVQSTS IPSSVAGERT TKFNGSGKTK RAVTMLCNAQ SSSLTLRDFT GLRGCNAIDT
     LVRSGETLQS KVAAATYVRR PRGCRFVPKA MFERFTEKAI KVIMLAQEEA RRLGHNFVGT
     EQILLGLIGE GTGIAAKVLK SMGINLKDAR VEVEKIIGRG SGFVAVEIPF TPRAKRVLEL
     SLEEARQLGH NYIGSEHLLL GLLREGEGVA ARVLENLGAD PSNIRTQVIR MVGESNEAVG
     ASVGGGTSGQ KMPTLEEYGT NLTKLAEEGK LDPVVGRQPQ IERVTQILGR RTKNNPCLIG
     EPGVGKTAIA EGLAQRIANG DVPETIEGKK VITLDMGLLV AGTKYRGEFE ERLKKLMEEI
     KQSDEIILFI DEVHTLIGAG AAEGAIDAAN ILKPALARGE LQCIGATTLD EYRKHIEKDP
     ALERRFQPVK VPEPTVDETI QILKGLRERY EIHHKLRYTD EDLVAAAQLS YQYISDRFLP
     DKAIDLIDEA GSRVRLRHAQ LPEEAKELEK ELRQITKEKN EAVRGQDFEK AGELRDREMD
     LKAQITALID KNKEVSKAES EAADTGPLVT EADIQHIVSS WTGIPVEKVS TDESDRLLKM
     EETLHTRIIG QDEAVKAISR AIRRARVGLK NPNRPIASFI FSGPTGVGKS ELAKALAAYY
     FGSEEAMIRL DMSEFMERHT VSKLIGSPPG YVGYTEGGQL TEAVRRRPYT VVLFDEIEKA
     HPDVFNMMLQ ILEDGRLTDS KGRTVDFKNT LLIMTSNVGS SVIEKGGRRI GFDLDLDEKD
     SSYNRIKSLV TEELKQYFRP EFLNRLDEMI VFRQLTKLEV KEIADIMLKE VFERLKVKEI
     ELQVTERFRD RVVDEGYNPS YGARPLRRAI MRLLEDSMAE KMLANEIKEG DSVIVDVDSD
     GNVTVLNGSS GTPSDPAPEP IPV