ID   CLPL_STAA8              Reviewed;         701 AA.
AC   Q2FV74;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, 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=SAOUHSC_02862;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=15554981; DOI=10.1111/j.1365-2958.2004.04368.x;
RA   Frees D., Chastanet A., Qazi S., Soerensen K., Hill P., Msadek T.,
RA   Ingmer H.;
RT   "Clp ATPases are required for stress tolerance, intracellular replication
RT   and biofilm formation in Staphylococcus aureus.";
RL   Mol. Microbiol. 54:1445-1462(2004).
CC   -!- FUNCTION: Required for the development of induced thermotolerance and
CC       intracellular multiplication within bovine mammary epithelial cells.
CC       {ECO:0000269|PubMed:15554981}.
CC   -!- DEVELOPMENTAL STAGE: Induced at the transition to stationary phase.
CC       {ECO:0000269|PubMed:15554981}.
CC   -!- INDUCTION: Expression is sigma B-dependent.
CC       {ECO:0000269|PubMed:15554981}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpL subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000253; ABD31861.1; -; Genomic_DNA.
DR   RefSeq; WP_001058981.1; NZ_LS483365.1.
DR   RefSeq; YP_501318.1; NC_007795.1.
DR   AlphaFoldDB; Q2FV74; -.
DR   SMR; Q2FV74; -.
DR   STRING; 1280.SAXN108_2798; -.
DR   EnsemblBacteria; ABD31861; ABD31861; SAOUHSC_02862.
DR   GeneID; 3921534; -.
DR   KEGG; sao:SAOUHSC_02862; -.
DR   PATRIC; fig|93061.5.peg.2587; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_3_9; -.
DR   OMA; GRVIQEH; -.
DR   PRO; PR:Q2FV74; -.
DR   Proteomes; UP000008816; 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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome; Virulence.
FT   CHAIN           1..701
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpL"
FT                   /id="PRO_0000269494"
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;  FBC87C248EE580B1 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
     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