ID   CLPL_STAA3              Reviewed;         701 AA.
AC   Q2FDV8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpL;
GN   Name=clpL; OrderedLocusNames=SAUSA300_2486;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
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; CP000255; ABD22319.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2FDV8; -.
DR   SMR; Q2FDV8; -.
DR   PRIDE; Q2FDV8; -.
DR   EnsemblBacteria; ABD22319; ABD22319; SAUSA300_2486.
DR   KEGG; saa:SAUSA300_2486; -.
DR   HOGENOM; CLU_005070_4_3_9; -.
DR   Proteomes; UP000001939; 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_0000269495"
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;  77852 MW;  66EF4765616AD926 CRC64;
     MNNGFFNSDF DSIFRRMMKD MQGSNQVGNK KYYINGKEVS PEELAQLTQQ GGNHSAEQSA
     QAFQQAAQRQ QGQQGGNGNY LEQIGRNLTQ EARDGLLDPV IGRDKEIQET AEVLSRRTKN
     NPILVGEAGV GKTAIVEGLA QAIVEGNVPA AIKDKEIISV DISSLEAGTQ YRGAFEENIQ
     KLIEGVKSSQ NAVLFFDEIH QIIGSGATGS DSGSKGLSDI LKPALSRGEI SIIGATTQDE
     YRNNILKDSA 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