CLPL_STAAM
ID CLPL_STAAM Reviewed; 701 AA.
AC Q99R88;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpL;
GN Name=clpL; OrderedLocusNames=SAV2548;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB58710.1; -; Genomic_DNA.
DR RefSeq; WP_001058993.1; NC_002758.2.
DR AlphaFoldDB; Q99R88; -.
DR SMR; Q99R88; -.
DR World-2DPAGE; 0002:Q99R88; -.
DR PaxDb; Q99R88; -.
DR EnsemblBacteria; BAB58710; BAB58710; SAV2548.
DR KEGG; sav:SAV2548; -.
DR HOGENOM; CLU_005070_4_3_9; -.
DR OMA; GRVIQEH; -.
DR PhylomeDB; Q99R88; -.
DR BioCyc; SAUR158878:SAV_RS13900-MON; -.
DR Proteomes; UP000002481; 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_0000269498"
FT DOMAIN 336..371
FT /note="UVR"
FT REGION 45..81
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; 77857 MW; 42CF6EE6C5703CE0 CRC64;
MNNGFFNSDF DSIFRRMMQD MQGSNQVGNK KYYINGKEVS PEELAQLTQQ GSNQSAEQSA
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