GenomeNet

Database: UniProt
Entry: A0A1M5GEX9_9FLAO
LinkDB: A0A1M5GEX9_9FLAO
Original site: A0A1M5GEX9_9FLAO 
ID   A0A1M5GEX9_9FLAO        Unreviewed;       890 AA.
AC   A0A1M5GEX9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05444344_2411 {ECO:0000313|EMBL:SHG02305.1};
OS   Tenacibaculum mesophilum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=104268 {ECO:0000313|EMBL:SHG02305.1, ECO:0000313|Proteomes:UP000183998};
RN   [1] {ECO:0000313|EMBL:SHG02305.1, ECO:0000313|Proteomes:UP000183998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13764 {ECO:0000313|EMBL:SHG02305.1,
RC   ECO:0000313|Proteomes:UP000183998};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQVV01000004; SHG02305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5GEX9; -.
DR   STRING; 104268.SAMN05444344_2411; -.
DR   Proteomes; UP000183998; 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:SHG02305.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHG02305.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          26..167
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          433..544
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   890 AA;  100514 MW;  A8A2D01303DD2142 CRC64;
     MSLVLKKNQL VLNLTFIEKN KNDMNFNNYT IKSQETIQQA QQLAQSYGNN LIENEHIFKA
     LFLVDENVLP FILKKLNINV TVIQQILDKQ LESFSKVTGA DLMLSREANK TLNEASIIAK
     KMNDEYVSIE HLILAIFKSK SQIAQVLKDQ GVSEKSLKAA IEELRKGNRV TSQSAEETYN
     SLNKYAKNLN QLAQDGKLDP VIGRDEEIRR LLQILSRRTK NNPILVGEPG TGKTAIAEGL
     AHRIIRGDVP ENLKEKQIFS LDMGALIAGA KYKGEFEERL KSVVKEVTKS EGDIVLFIDE
     IHTLVGAGGG QGAMDAANIL KPALARGELR AIGATTLDEY QKYFEKDKAL ERRFQKVMVD
     EPDTESAISI LRGIKDKYET HHKVRIKDEA IIGAVELSQR YITNRFLPDK AIDLMDEAAS
     KLRMEINSKP EELDVLDRKI MQLEIEIEAI KRENDETKLK SLNADLANLK EERNEINAKW
     QSEKSVVDTI QNLKTDIENY KHEAEKAERN GDYGKVAELR YGKIKEAQEE LDKQQDILAN
     QQGNSLIKEE VTYDDIAEVV AKWTGVPVTK MLQSEREKLL KLEDELHKRV VGQEEAIEAV
     SDAVRRSRSG LQNPDKPIGS FLFLGTTGVG KTELAKALAE YLFDDENAMT RIDMSEYQER
     HSVSRLVGAP PGYVGYDEGG QLTEAVRRKP YSVVLLDEIE KAHPDTFNIL LQVLDEGRLT
     DNKGRIADFK NTIIIMTSNM GSHIIQEKFD NMKGDIDTTI DLAKTEVLGL LKQSVRPEFL
     NRIDDIIMFT PLSENNIKEI VKLQLNNVKK MIAQQNIIFD ATDEAINYLA TKGYQPEFGA
     RPVKRVIQKE VLNQLSKEIL SGQVTTDSII LLDAFDDELV FRNQSDLVNN
//
DBGET integrated database retrieval system