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Database: UniProt
Entry: A0A174QFH7_9CLOT
LinkDB: A0A174QFH7_9CLOT
Original site: A0A174QFH7_9CLOT 
ID   A0A174QFH7_9CLOT        Unreviewed;       867 AA.
AC   A0A174QFH7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=CP373A1_09650 {ECO:0000313|EMBL:OBY10761.1};
OS   Clostridium paraputrificum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=29363 {ECO:0000313|EMBL:OBY10761.1, ECO:0000313|Proteomes:UP000092714};
RN   [1] {ECO:0000313|EMBL:OBY10761.1, ECO:0000313|Proteomes:UP000092714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=373-A1 {ECO:0000313|EMBL:OBY10761.1,
RC   ECO:0000313|Proteomes:UP000092714};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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. {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, 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:OBY10761.1}.
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DR   EMBL; MAPZ01000019; OBY10761.1; -; Genomic_DNA.
DR   RefSeq; WP_027096848.1; NZ_MAPZ01000019.1.
DR   AlphaFoldDB; A0A174QFH7; -.
DR   GeneID; 42774686; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000092714; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
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   NCBIfam; TIGR03346; chaperone_ClpB; 1.
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|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092714};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          417..497
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   867 AA;  98024 MW;  E4F6F58CEB94FA31 CRC64;
     MNVDKMTIRV QQALNDANLI AVKYNHQQIE VIHLFAALVE QEDGLIPNIL TKMNVDVRGL
     KSTLNRTLDN MPKVLGEGAN SSGVYITRKV EEVLIKAEEL AKKFEDSYIS VEHLMLAILD
     KEKSGAVGDI LKSYSITEKN FMKVLSEVRG SQRVETNDPE GTYDALAKYG TNLVELAKKH
     KLDPVIGRDE EIRRAVRILS RRTKNNPVLI GEPGVGKTAI VEGLAERIVR GDVPEGLKDK
     IIFSLDMGSL IAGAKYRGEF EERLKAVLKE VQNSEGRIIL FIDEIHTIVG AGKTDGAMDA
     GNLIKPLLAR GELHCIGATT FDEYRQYIEK DKALERRFQP VIVDEPSVDD TISILRGLKE
     KFEIHHGIRI HDSAIVAAAK LSNRYIQDRY LPDKAIDLID EAGSMIRSEI DSLPTELDVI
     RRKVFQLEIE KEALEKEKDE GSKKRLEALT KELAELKEKN DEMTAKYEKE KEHITSLKDL
     KTKLDEARGD LERYEREYDY NKVAEIRYSV IPKIEEEIKT KEAEVKENYE GALLKEEVTE
     EEISEVLSKW TGIPVSNLLE GEREKLLRLD SELQKRVIGQ DAAVEAVSNA ILRARAGLKD
     VNKPIGSFIF LGPTGVGKTE LAKTLARTMF DSEDAMIRID MSEYMEKHAV SRLVGAPPGY
     VGYEQGGQLT EAVRRKPYSV LLFDEIEKAH EDVFNMFLQI LDDGRLTDNK GKTVDFKNTI
     IIMTSNIGSQ YLLDNQGDEI TDESKDKVMA SLRNKFKPEF LNRVDDIIMF KPLSEEGIKK
     IIDIFLDEVR ARLVDKNIKL EVTDEAKSIL AKEGYDPVYG ARPLKRYIQN TLENNLARRI
     IKGDVHYGST VVVDGQNNEL TLYTREK
//
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