ID   CLPA_PINPS              Reviewed;          30 AA.
AC   P81671;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA homolog;
DE   Flags: Fragments;
OS   Pinus pinaster (Maritime pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=71647;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Needle;
RX   PubMed=10344291;
RX   DOI=10.1002/(sici)1522-2683(19990101)20:4/5<1098::aid-elps1098>3.0.co;2-z;
RA   Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A.,
RA   Frigerio J.-M., Plomion C.;
RT   "Separation and characterization of needle and xylem maritime pine
RT   proteins.";
RL   Electrophoresis 20:1098-1108(1999).
CC   -!- FUNCTION: May interact with a ClpP-like protease involved in
CC       degradation of denatured proteins in the chloroplast. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein (spot
CC       n9) is: 5.9, its MW is: 92 kDa.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR   AlphaFoldDB; P81671; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Chloroplast; Direct protein sequencing;
KW   Nucleotide-binding; Plastid; Repeat.
FT   CHAIN           <1..>30
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpA
FT                   homolog"
FT                   /id="PRO_0000191214"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         30
SQ   SEQUENCE   30 AA;  2923 MW;  44B5950B73A96152 CRC64;
     AESEAGDASP LVTEVLIGSP PGYVGYTEGG