ID   CLPL_STAAW              Reviewed;         701 AA.
AC   Q8NUR7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpL;
GN   Name=clpL; OrderedLocusNames=MW2469;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Required for the development of induced thermotolerance.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpL subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BA000033; BAB96334.1; -; Genomic_DNA.
DR   RefSeq; WP_001058988.1; NC_003923.1.
DR   AlphaFoldDB; Q8NUR7; -.
DR   SMR; Q8NUR7; -.
DR   EnsemblBacteria; BAB96334; BAB96334; BAB96334.
DR   KEGG; sam:MW2469; -.
DR   HOGENOM; CLU_005070_4_3_9; -.
DR   OMA; GRVIQEH; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR001270; ClpA/B.
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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN           1..701
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpL"
FT                   /id="PRO_0000269502"
FT   DOMAIN          336..371
FT                   /note="UVR"
FT   REGION          47..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..332
FT                   /note="I"
FT   REGION          383..575
FT                   /note="II"
FT   BINDING         126..133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         457..464
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   701 AA;  77836 MW;  E8688D377CF1FF4C CRC64;
     MNNGFFNSDF DSIFRRMMQD MQGSNQVGNK KYYINGKEVS PEELAQLTQQ GGNHSAEQSA
     QAFQQAAQRQ QGQQGGNGNY LEQIGRNLTQ EARDGLLDPV IGRDKEIQET AEVLSRRTKN
     NPILVGEAGV GKTAIVEGLA QAIVEGNVPA AIKDKEIISV DISSLEAGTQ YRGAFEENIQ
     KLIEGVKSSQ NAVLFFDEIH QIIGSGATGS DSGSKGLSDI LKPALSRGEI SIIGATTQDE
     YRNNILKDAA LTRRFNEVLV NEPSAKDTVE ILKGIREKFE EHHQVKLPDD VLKACVDLSI
     QYIPQRLLPD KAIDVLDITA AHLSAQSPAV DKVETEKRIS ELENDKRKAV SAEEYKKADD
     IQNEIKSLQD KLENSNGEHT AVATVHDISD TIQRLTGIPV SQMDDNDIER LKNISNRLRS
     KIIGQDQAVE MVSRAIRRNR AGFDDGNRPI GSFLFVGPTG VGKTELAKQL AIDLFGNKDA
     LIRLDMSEYS DTTAVSKMIG TTAGYVGYDD NSNTLTEKVR RNPYSVILFD EIEKANPQIL
     TLLLQVMDDG NLTDGQGNVI NFKNTIIICT SNAGFGNGND AEEKDIMHEM KKFFRPEFLN
     RFNGIVEFLH LDKDALQDIV NLLLDDVQVT LDKKGITMDV SQDAKDWLIE EGYDEELGAR
     PLRRIVEQQV RDKITDYYLD HTDVKHVDID VEDNELVVKG K