ID A0A255T3M2_9BACT Unreviewed; 875 AA.
AC A0A255T3M2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=CIK99_01440 {ECO:0000313|EMBL:OYP59824.1};
OS Prevotella sp. P5-92.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2024222 {ECO:0000313|EMBL:OYP59824.1, ECO:0000313|Proteomes:UP000216769};
RN [1] {ECO:0000313|EMBL:OYP59824.1, ECO:0000313|Proteomes:UP000216769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P5-92 {ECO:0000313|EMBL:OYP59824.1,
RC ECO:0000313|Proteomes:UP000216769};
RA Accetto T., Nograsek B., Avgustin G.;
RT "Comparative genomics of non-oral Prevotella species.";
RL Submitted (AUG-2017) 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:OYP59824.1}.
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DR EMBL; NPJG01000007; OYP59824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255T3M2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000216769; 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; IPR017729; ATPase_T6SS_ClpV1.
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 NCBIfam; TIGR03345; VI_ClpV1; 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:UP000216769};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 403..537
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 875 AA; 98917 MW; 1B8350A83D1ED304 CRC64;
MTLDKFTIKA QETVQEAVNL AQSSGQQSIE PVHLLKAIMT KAKDVSNFIF QKLGVNSRQV
EMLIDSEISH LPRVQGGQPY LSADTNQTLQ RAVETAQKMG DQFVSVEPIL LAIVASNSTA
SRILKDAGCS EKEMRKAINE LRQGQKVESQ SADDNYQSLA KYAKNLVEEA RNGKLDPVIG
RDDEIRRVLQ ILSRRTKNNP ILIGEPGTGK TAIVEGLAER IVRGDVPENL KDKQLYSLDM
GALVAGAKYK GEFEERLKSV INEVTKSDGR IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRSIG ATTLNEYQKY FEKDKALERR FQTVMVDEPD ELSAISILRG LKERYENHHK
VRIQDDACIA AVKLSERYIS DRFLPDKAID LMDEAAAKLR MERDSVPEEL DEITRRLKQL
EIEREAIKNE QARNKDEESS SEGKLAQLDK DIAELRDKEK AFRAKWEGEK ALVNRIQDDK
QQMENLKLEA ERAEREGNYE RVAEIRYSKL KMLEDDIKHI QQQLKNAQGA EAMVREEVTE
DDIAEVVSRW TGIPVTRMLQ SEREKLLHLE EELHKRVIGQ EEAISAVSDA VRRSRAGLQD
PKRPIASFIF LGTTGVGKTE LAKALAEYLF NDETMMTRID MSEYQEKFSV SRLIGAPPGY
VGYDEGGQLT EAVRRKPYSV VLFDEIEKAH PDVFNILLQV LDDGRLTDNK GRTVNFKNTI
IIMTSNLGSQ MINDEIRRKT ETLGNTLDEG FIITLKNKIL DMLKQTIRPE FLNRIDETIM
FLPLRKDEIA NVVRLQMNAV KRMLEPQGFE LNITDAAVDI LAQEGFDPEF GARPVKRAIQ
RCVLNELSRK ILSEEVSREK PITIDAVGEQ LVFRN
//