CLPL_STAAR
ID CLPL_STAAR Reviewed; 701 AA.
AC Q6GDQ0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpL;
GN Name=clpL; OrderedLocusNames=SAR2628;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG41607.1; -; Genomic_DNA.
DR RefSeq; WP_001063330.1; NC_002952.2.
DR AlphaFoldDB; Q6GDQ0; -.
DR SMR; Q6GDQ0; -.
DR KEGG; sar:SAR2628; -.
DR HOGENOM; CLU_005070_4_3_9; -.
DR OMA; GRVIQEH; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000000596; 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_0000269500"
FT DOMAIN 336..371
FT /note="UVR"
FT REGION 46..78
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; 77984 MW; 70CA3B3BE776D2C8 CRC64;
MNNNFFNSDF DSILRRMMQD MQNSNQTSNK KYYINGKEVS PEELAQFTQQ GGNHSAEQSA
QAFQQAALRQ QGQQSGNGNY LEQIGRNLTQ EARDGLLDPV IGRDKEIQET AEVLSRRTKN
NPILVGEAGV GKTAIVEGLA QAIVEGNVPA AIKDKEIISI DISSLEAGTQ YRGAFEENIQ
KLVEGVKSSQ NAVLFFDEIH QIIGSGATGS DSGSKGLSDI LKPALSRGEI SIIGATTQDE
YRNNIMKDAA LTRRFNEVLV NEPSAKDTVE ILKGIREKFE THHQVKLPDD VLKACVDLSI
QYIPQRLLPD KAIDVLDITA AHLSAQSPAI DKVTTEKRIS ELEHDKRKAV SAEEYKKADD
IQKEIKSLQD KLENSNGEHT AVATVHDISD TIQRLTGIPV SQMDANDIER LKNISSRLRS
KIIGQDKAVE MVSRAIRRNR AGFDDGNRPI GSFLFVGPTG VGKTELAKQL AIDLFGNKEA
LIRLDMSEYS DTTAVSKMIG TTAGYVGYDD NSNTLTEKVR RNPYSVILFD EIEKANPQIL
TLLLQVMDDG NLTDGQGNVI NFKNTIIICT SNAGFGNGND TEEKDIMHEM KKFFRPEFLN
RFNGIVEFLH LDKDALQDIV NLLLDDVQVT LDKKGITMDV SQDAKDWLIE EGYDEELGAR
PLRRIVEQQV RDKITDYYLD HTDVKHVDID VEDNELVVKG K