ID   CLPL_STAAB              Reviewed;         702 AA.
AC   Q2YWB1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpL;
GN   Name=clpL; OrderedLocusNames=SAB2423;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI82111.1; -; Genomic_DNA.
DR   RefSeq; WP_001063340.1; NC_007622.1.
DR   AlphaFoldDB; Q2YWB1; -.
DR   SMR; Q2YWB1; -.
DR   PRIDE; Q2YWB1; -.
DR   KEGG; sab:SAB2423; -.
DR   HOGENOM; CLU_005070_4_3_9; -.
DR   OMA; GRVIQEH; -.
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..702
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpL"
FT                   /id="PRO_0000269496"
FT   DOMAIN          336..371
FT                   /note="UVR"
FT   REGION          46..80
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   702 AA;  78093 MW;  63E95C8FA03EDDC3 CRC64;
     MNNNFFNSDF DSILRRMMQD MQNSNQTSNK KYYINGKEVS QEELAQFTQQ GGNHSAEQSA
     QAFQQAALRQ QGQQSGNGNY LEQIGRNLTQ EARDGLLDPV IGRDKEIQET AEVLSRRTKN
     NPILVGEAGV GKTAIVEGLA QAIVEGNVPA AIKDKEIISI DISSLEAGTQ YRGAFEENIQ
     KLVEGVKSSQ NAVLFFDEIH QIIGSGATGS DSGSKGLSDI LKPALSRGEI SIIGATTQDE
     YRNNILKDAA LTRRFNEVLV NEPSAKDTVE ILKGIREKFE THHQVKLPDD VLKACVDLSI
     QYIPQRLLPD KAIDVLDITA AHLSAQSPAI DKVATEKRIS ELEHDKRKAV SAEEYKKADD
     IQNEIKSLQD KLENSNGEHT AVATVHDISD TIQRLTGIPV SQMDANDIER LKNISSRLRS
     KIIGQDKAVE MVSRAIRRNR AGFDDGNRPI GSFLFVGPTG VGKTELAKQL AIDLFGNKEA
     LIRLDMSEYS DTTAISKMIG TTAGYVGYDD NSNTLTEKVR RNPYSVILFD EIEKANPQIL
     TLLLQVMDDG NLTDGQGNVI NFKNTIIICT SNAGFGNGTD QEYDDIMQEM KKFFRPEFLN
     RFNGIVEFLH LDKDALQDIV NLLLDDVQVT LDKKGITMNV SQDAKDWLIE EGYDEELGAR
     PLRRIVEQQV RDKITDYYLD HTDVKHVDLD IEDNELVVKG KS