ID H3NDY1_9LACT Unreviewed; 740 AA.
AC H3NDY1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN ORFNames=HMPREF9703_00762 {ECO:0000313|EMBL:EHR33708.1};
OS Dolosigranulum pigrum ATCC 51524.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Dolosigranulum.
OX NCBI_TaxID=883103 {ECO:0000313|EMBL:EHR33708.1, ECO:0000313|Proteomes:UP000003599};
RN [1] {ECO:0000313|EMBL:EHR33708.1, ECO:0000313|Proteomes:UP000003599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51524 {ECO:0000313|EMBL:EHR33708.1,
RC ECO:0000313|Proteomes:UP000003599};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dolosigranulum pigrum ATCC 51524.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHR33708.1}.
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DR EMBL; AGEF01000007; EHR33708.1; -; Genomic_DNA.
DR RefSeq; WP_004635764.1; NZ_JH601103.1.
DR AlphaFoldDB; H3NDY1; -.
DR STRING; 29394.BWX42_04555; -.
DR PATRIC; fig|883103.3.peg.748; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_9; -.
DR Proteomes; UP000003599; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003599};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 38..72
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 740 AA; 83015 MW; CBFDD162AE10F6D6 CRC64;
MNYTAGVELA VEKARQKAYD QSHRRLEIPH MWSVLIEEER TQAIYQELQV DLEKLQEVVE
AEMAKLSTTS KEQSPQDKQM SHQLYHVFKD ARDLATKYEY ESINIDLLLV SVMNRYYHPI
VQEIAQYGIG RAEIFRAIRI LNGESNMSEE SEERYLDQYA VNLSALNRQG EIGHVVGRDE
ETDHMIQILS RKTKNNPILI GEPGVGKTAI VEGLTARLAS TEAPANLQGA TIYSLSLGAL
VAGASFRGEF EARMKAVLEE LQAEEKAILF IDEIHTIVGA GNAEGSLDAG NLMKPLLARG
TIKVIGSTTR AEYRKHFQKD RALVRRFQPI QIKEPSVEET ITILRGIRPE YEAFHQLSIS
DEALELSATL SKRYIPERHL PDKAIDVMDE AAAKLRITTE IDTAKRVVDD QAIYSLIAKK
TGIPVHKLQS DERKQLMHLE ETLSSQVIGQ TEAVSAVSDA IIRSRVGIQD PNRPLGSFLF
LGPTGVGKTE LAKVLARELF ESEDNMIRLD MSEYMEKHSV SQLIGSPPGY VGHDDGGQLT
EAVRFNPYSI ILFDEVEKAH KDVFNLLLQV LDDGVLTDAK GRRVDFKNTI LILTSNIGAH
LLLDQVKAGD DTPEISSEVR EALHEMLRQH FRPEFLNRID EVVTFKPLSM AVMAGIVELQ
LATLQERLQA QNIVLAITDQ AKKWIAQEAY DPAYGARPIR RFLTTHLETP IAKMIIAEEI
EAGQQLTIDV TDESLKINVQ
//