ID Q2LUK2_SYNAS Unreviewed; 874 AA.
AC Q2LUK2;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 24-JAN-2024, entry version 135.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SYN_02525 {ECO:0000313|EMBL:ABC77760.1};
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC77760.1, ECO:0000313|Proteomes:UP000001933};
RN [1] {ECO:0000313|EMBL:ABC77760.1, ECO:0000313|Proteomes:UP000001933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB {ECO:0000313|EMBL:ABC77760.1,
RC ECO:0000313|Proteomes:UP000001933};
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC77760.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2LUK2; -.
DR STRING; 56780.SYN_02525; -.
DR KEGG; sat:SYN_02525; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_7; -.
DR InParanoid; Q2LUK2; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000001933; Chromosome.
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:UP000001933};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 14..157
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 416..544
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 874 AA; 98839 MW; 41CCA4248C59E720 CRC64;
MIMRNQRGGE IMRFDKFTLK VLEGLQEAQT LAGNYGHHGI DVEHLLLAFI AQPEGIVGNI
LKKLGTEPAQ IEKEIKKVVE RLPRISGPIQ SYITPRLNKI LDNAMTEAAH LNDEYVSAEH
VLIAMANEKE GEASRILRSA GVTRDNIFKV LVEIRGTQRI TDPNPEEKYE ALKRYAKDFN
ELARKGAFDP VIGRNDEIRR IMQVLSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVNGDVP
ESLKNKRVIG LDIGALVAGA KYRGEFEDRL KAVLKEVTDA QGEIILFIDE IHTVVGAGAA
EGSVDASNML KPALARGELR CVGATTLNEY RKHIEKDPAL ERRFQPILVR EPTVEDTIAI
LRGLKERYEI HHGVRIKDSA IVAAATLSNR YISDRFLPDK AVDLVDEAAS RLRIELDSLP
AEIDVLERKA IQLEIERQSL KNETDRTSLE RREKIERELA DLRESMNSMK LHWSEEKEVI
KRIQTIKSDL ENFKNEEQNA MREGNLARAA EIRYGKLVEL NRALEEEQNR LKEIQKDSKM
LKEEVDAEDV AEVVANWTGI PVARMMESDI QKLIHMEDRL KQRVIGQDEG IHAVSAALRR
ARSGLQDPNR PIGSFIFLGP TGVGKTELAR ALAEFMFDNE QAMIRIDMSE YMEKHSVARL
IGAPPGYVGY DEGGYLTEAV RRRPYAVLLF DEIEKAHPDV FNILLQILDD GRLTDGHGRT
VDFKNTIVIL TSNVGSQWIQ DITLTAEEKR LRTMEILRAT FKPEFLNRID DIIIFRSLTM
TDLERIIAIQ IGLIQKRLMD RKLFLELTEK AKNYISQEGY SPVYGARPLK RALQKMLLDN
LSMKILEGAF VEGDHILADI DDRGEINFTK KSGS
//