ID F3ZTM6_9BACE Unreviewed; 863 AA.
AC F3ZTM6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=Bcop_1050 {ECO:0000313|EMBL:EGJ71257.1};
OS Bacteroides coprosuis DSM 18011.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ71257.1, ECO:0000313|Proteomes:UP000018439};
RN [1] {ECO:0000313|EMBL:EGJ71257.1, ECO:0000313|Proteomes:UP000018439}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ71257.1,
RC ECO:0000313|Proteomes:UP000018439};
RX PubMed=21677860; DOI=10.4056/sigs.1784330;
RA Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Non-contiguous finished genome sequence of Bacteroides coprosuis type
RT strain (PC139).";
RL Stand. Genomic Sci. 4:233-243(2011).
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; CM001167; EGJ71257.1; -; Genomic_DNA.
DR RefSeq; WP_006744414.1; NZ_CM001167.1.
DR AlphaFoldDB; F3ZTM6; -.
DR STRING; 679937.Bcop_1050; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_10; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000018439; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000018439};
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 396..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 97465 MW; 5F9B1AE7398192EC CRC64;
MNLNSYTIKS QEAIQETVQL VQQNNQQIIE PLHLLLGVMN VGEDVVNFIL QKLGVNKDFV
IQQTESKVKS LPKVTGGNPT LSNEANEVLI KAVDLAKEMG DEFASIEQLF LAILKVKSSA
STLLKDAGVV EDKVRSAITE LRKGSKVTSQ SGDDNYLSLD KYAINLIDAA RDGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP ILIGEPGTGK TAIVEGLANR ILRGDVPDNL KDKQLFSLDM
GALIAGAKYK GEFEERLKSV VNEVKKSEGN IILFIDEIHT LVGAGKSDGA MDAANILKPA
LARGELRSIG ATTLDEYQKY FEKDKALERR FQIVQVDEPD IDSSISILRG LKERYENHHH
VRIKDDAIIA AVELSNRYIT DRFLPDKAID LMDEAAAKLR MEINSLPEEL DEISRKLMQL
EIEKAAIKRE NDTKKLEQLT KEIAELKEQE SSYKAKWEHE RGLVNKIQHN KSEIEHLKYE
ADKAEREGDY GKVAEIRYGK IQQLNKEIEE TQDNLHKIQK GNALIREEVE AEDIADIVSR
WTGIPVNKML QSEKEKLLHL EEELHKRVVG QDEAIEAVSD AVRRSRAGLQ DPRRPIGSFI
FLGTTGVGKT ELAKALAEFL FDDETMMTRI DMSEYQEKHS VSRLVGAPPG YVGYEEGGQL
TEAIRRKPYS VVLFDEIEKA HPDVFNILLQ VLDDGRLTDN KGRLVNFKNT IIIMTSNMGS
GYIQEQMSRI NEVSDKEALI EETKQGVMDM LKKTIRPEFL NRIDETIMFL PLNENQIKQI
VMLQIKQVQK MVAENGMNLQ LTDNAIGFLA EKGYNPEFGA RPAKRAIQRY LLNDLSKKIL
AQEIDQAKPI IIDQENDHLV FKN
//
