ID A0A1M5NCC4_9BACT Unreviewed; 871 AA.
AC A0A1M5NCC4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04488109_2221 {ECO:0000313|EMBL:SHG86839.1};
OS Chryseolinea serpens.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Chryseolinea.
OX NCBI_TaxID=947013 {ECO:0000313|EMBL:SHG86839.1, ECO:0000313|Proteomes:UP000184212};
RN [1] {ECO:0000313|EMBL:SHG86839.1, ECO:0000313|Proteomes:UP000184212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24574 {ECO:0000313|EMBL:SHG86839.1,
RC ECO:0000313|Proteomes:UP000184212};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQWQ01000001; SHG86839.1; -; Genomic_DNA.
DR RefSeq; WP_073133629.1; NZ_FQWQ01000001.1.
DR AlphaFoldDB; A0A1M5NCC4; -.
DR STRING; 947013.SAMN04488109_2221; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000184212; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:SHG86839.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHG86839.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184212};
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 82..109
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 396..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 98255 MW; 9FA0EDD46D1C6979 CRC64;
MNFEKFTIKS QEALQKSAEI AMAKQQQAIE PGHILKAILE TDENVSNYLF KKLNVSETIL
HNKLEDLLNS YPHVQGQQPY LSSASNTVLQ NAEKELREFK DEFIAVEHLL LALLGSKDKV
SSVLKDAGLE RSSLIKAIKE LRGGASVTDQ NAEAKYKSLE RYSKNLNDLA KRGKIDPVIG
RDEEIRRVLQ ILSRRTKNNP ILLGEPGVGK TAIVEGMAQR IVDGDVPENL KDKILVSLDM
GLLVAGAKYK GEFEERLKAV IKEVTDANGQ IILFIDEIHT LIGAGGGEGA MDAANLLKPA
LARGELHAIG ATTLKEYQKY IEKDKALERR FQSVMVDEPS VEDSISILRG IKDKYELHHG
VRIKDDAVIA AVELSSRYIS DRFLPDKAID LMDEAASKLR LEMDSLPEEL DELNRKIMQL
EIEREAIRRE RDKEKEHLLS KEIAELSEQR NSLKARWESE KQVVHGIQKE KESIDKLKFE
AEHAEKAGDY GKVAEIRYGK ITEAEKRLVE AEEKMKAMQG EKNLLKEEVD SEDIAEVVAK
WTGIPVSKML QSEREKLLHL EDELSKRVAG QEEAITALSD AVRRSRAGLQ DPKRPIGSFI
FMGTTGVGKT ELSKALADYL FNDDSAMVRI DMSEYQERHS VSRLIGAPPG YVGYDEGGQL
TEAVRRKPYS VILLDEIEKA HPDVFNILLQ VLDEGRLTDN KGRVANFKNT IIIMTTNIGS
QLIQENFEKI TPENYFDVLE DTKDEVLALL RKSVRPEFVN RIDEIIMFRP LSQKDIRKIV
DIQVGLIVKR LEEAGVKIEI SDSARDRMAK LGYDPQFGAR PLKRVMQREI LNELSKQILA
GKVQKDSVIF IDLKNETDFV FENLEAAEVV K
//