GenomeNet

Database: UniProt
Entry: H3NDY1_9LACT
LinkDB: H3NDY1_9LACT
Original site: H3NDY1_9LACT 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system