ID F4C242_SPHS2 Unreviewed; 865 AA.
AC F4C242;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Sph21_3149 {ECO:0000313|EMBL:ADZ79692.1};
OS Sphingobacterium sp. (strain 21).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ79692.1};
RN [1] {ECO:0000313|EMBL:ADZ79692.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21 {ECO:0000313|EMBL:ADZ79692.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT "Complete sequence of Sphingobacterium sp. 21.";
RL Submitted (MAR-2011) 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}.
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DR EMBL; CP002584; ADZ79692.1; -; Genomic_DNA.
DR AlphaFoldDB; F4C242; -.
DR STRING; 743722.Sph21_3149; -.
DR KEGG; shg:Sph21_3149; -.
DR PATRIC; fig|743722.3.peg.3368; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_10; -.
DR OrthoDB; 9803641at2; -.
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..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 97346 MW; 2F883865A4B251E9 CRC64;
MNLNNFTIKA QEAIQKASEI AGGNQHQAIE NAHLLKALLL VDENVVSHLL KKLNVNINRL
NEALDQQISG FPKVSGSNIY LSSSTNTALQ KAQGYLKDFK DDFVSVEHLL LGILNAGDKT
AAALKDQGVT EKDLKKAIIE LRGNTRVTDQ NAEATYNALN KYARNLNEFA ESGKLDPVIG
RDEEIRRVIQ ILSRRTKNNP ILVGEPGVGK TAIAEGIAHR IIKGDVPENL KSKTVFSLDM
GALIAGAKYK GEFEERLKAV VKEVTDSDGE IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLNEFQKY FEKDKALERR FQKVMVDEPD TQDAISILRG IKERYETHHK
VRIKDEAIIA AVELSQRYIA DRFLPDKAID LMDEAASKLR LEMDSVPEAV DEIERKIMQL
EIEREAIKRE NDTHKVEELS REIANLASDR DSLRAAWQSE KSLVDNLNHH VQQIEDFKLE
AEQAERAGDY GKVAEIRYGR IKQAQDELEK LKKELEEKQG TGRMLKEEVT AEDIADVVSR
WTGIPVSKMV QSEREKLLHL EEELHKRVAG QSEAIEAISD AIRRSRAGLS DKRRPIGSFI
FLGTTGVGKT ELAKALAEFL FNDEHSMVRI DMSEYQERHA VSRLIGAPPG YVGYDEGGQL
TEAIRRRPYS VVLLDEIEKA HPDVFNILLQ VLDDGHLTDN KGRVVNFKNT IIIMTSNIGS
HLIQENFSEL NEINRDEIIA KTKNEVFELL KKSIRPEFLN RIDEVIMFTP LNRDEIGEIV
RLQFNGVQRQ LAEMGIQLEA SDEALDWLAQ LGYDPQFGAR PLKRVIQKRI LNELSKEILA
GKIDKDSKIK LDMFDHKFVF LQENS
//
