ID H3NID1_9LACT Unreviewed; 825 AA.
AC H3NID1;
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=HMPREF9708_00620 {ECO:0000313|EMBL:EHR37441.1};
OS Facklamia languida CCUG 37842.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=883113 {ECO:0000313|EMBL:EHR37441.1, ECO:0000313|Proteomes:UP000006190};
RN [1] {ECO:0000313|EMBL:EHR37441.1, ECO:0000313|Proteomes:UP000006190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 37842 {ECO:0000313|EMBL:EHR37441.1,
RC ECO:0000313|Proteomes:UP000006190};
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 Facklamia languida CCUG 37842.";
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 -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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:EHR37441.1}.
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DR EMBL; AGEG01000006; EHR37441.1; -; Genomic_DNA.
DR RefSeq; WP_006308647.1; NZ_JH601133.1.
DR AlphaFoldDB; H3NID1; -.
DR STRING; 883113.HMPREF9708_00620; -.
DR PATRIC; fig|883113.3.peg.621; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000006190; 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 Gene3D; 4.10.860.10; UVR domain; 1.
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; IPR028299; ClpA/B_CS2.
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; PF02861; Clp_N; 2.
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.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000006190};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 147..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 426..475
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 149..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 92004 MW; 1E251667489D90C1 CRC64;
MFEELFTESA RQAMLYAAEH AYYLRHQAVG TEHILLGLAR EERGIAGTIL REFGADYSEL
LHELEIIHGK VSQPRTQGEA IIPYSPRAKK VIMNASTDAK RLGAARVGTE HLLLALIKEE
ILATVLLKNL SIDLGQLRQA IFEEMGVSPQ KKSDQQNRRQ AKANKNQASD SPTPTLDSVS
RDLTQLARDN QLDPVIGREE EIRRMIQIIS RRTKNNPVLV GEPGVGKTAI AEGLAQAMVS
GKVPKELMTK RLMMLDTAAL VAGTKYRGEF EERMKKIIEE IAQEGQVILF IDELHTLMGA
GGAEGAIDAA NILKPALARG EIQTIGATTF DEYQKHIEKD AALERRFSKV VIDEPTPAES
IEIITGLRSK YEDHHQVEIT DEAIEAAVKL SARYLTERKL PDKAVDLIDE AAAKVRIERG
QDPYNIQELE VQLKAISKRK EQAILERNFD LAADLREEEV KVEEAIQKTA NKKKKTDQDQ
VVERPCVTSE EVSEVIAMAT GVPIHQMNLT ESKRLVHLEE ELHERVIGQD AAVSSVARAI
RRARSGLKSP QRPIGSFLFL GPTGVGKTEL AKTLADSMFG SQENMIRIDM SEYMEKHSIS
RMIGSPPGYV GYDEAGQLTE KVRQKPYSVI LLDEIEKAHP DVFNLLLQVF DDGQLTDGKG
RQVDFRNTII IMTSNLGATA LRDDKSVGFG AVDYSHDFKA MEARIMEELK RAFRPEFLNR
IDETIVFKSL TKDQIREIVK LHTAVIISRL ADMEIKARIT ETAVDIIAES GFDPEYGARP
IRRAIQKQIE DELSEMLLDG SIELGDQITI GGRSGSININ NRSKA
//