ID A0A3P1SYD1_9BACT Unreviewed; 861 AA.
AC A0A3P1SYD1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RRD02277.1};
GN ORFNames=EII32_03410 {ECO:0000313|EMBL:RRD02277.1};
OS Prevotella sp. OH937_COT-195.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2491051 {ECO:0000313|EMBL:RRD02277.1, ECO:0000313|Proteomes:UP000267043};
RN [1] {ECO:0000313|EMBL:RRD02277.1, ECO:0000313|Proteomes:UP000267043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH937_COT-195 {ECO:0000313|EMBL:RRD02277.1,
RC ECO:0000313|Proteomes:UP000267043};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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:RRD02277.1}.
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DR EMBL; RQZH01000005; RRD02277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1SYD1; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000267043; 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 78, MITOCHONDRIAL; 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 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 410..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 96894 MW; 2884324DDA5E4276 CRC64;
MTIDNFTIKA QESVQEAMNI TQRAGQQTLE PTHLLKGLLT KAKDIMNFLF QKTGVNGAHV
EQLVDSELSR QPRVQGGQPY LSNDANKVLV KAGEIAKSTG DEFVSVEPMI LALLSVNCTA
ARILKDAGMN ESDTRKAIEE LRQGQKVSSR SADENYQSLS KYAKNLVEDA RAGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP VLIGEPGTGK TAIVEGLAGR IVRGDVPENL KDKQLYSLDM
GALLAGAKYK GEFEERLKSV INEVTKSEGR IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRSIG ATTLNEYQKY FEKDKALERR FQTVMVDEPD ELSAISILRG LKERYENHHK
VRIQDDACIA AVKLSERYIS DRFLPDKAID LMDEAAAKMR MERDSVPEEL DDTMRQLKQL
EIEREAIKRE NDEGKLAQLD REIAGLREQE NTARAKWESE KGLVDKIQQD KQQIEQLKFE
ADRAEREGNY ARVAEIRYSS LKALEDDIAE LTKQLAQGND NRMVREEVTA DDIAEVVSRW
TGIPVTRMLQ NEREKLLHLE EELHRRVVGQ NEAITAVSDA VRRSRAGLQD PKRPLASFIF
LGTTGVGKTE LAKALAEYLF NDEHLMTRID MSEYQEKFSV SRLIGAPPGY VGYDEGGQLT
EAVRRKPYSV ILFDEIEKAH PDVFNILLQV LDDGRLTDNK GRTVNFKNTI IIMTSNLGSQ
YIQTEFAKMT DENRNAVINS TRETIMEMLK KTIRPEFLNR IDETIMFLPL SKDEITNVVR
MQVAAVQKIL AEQDVRLDLT DDAMNFLADA GFDPEFGARP VKRAIRRYVL NDLSKRLLAG
EVNRERPIVI DCDGNGLTFG N
//
