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Database: UniProt
Entry: A0A1M5NCC4_9BACT
LinkDB: A0A1M5NCC4_9BACT
Original site: A0A1M5NCC4_9BACT 
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
//
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