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Database: UniProt
Entry: A0A1M6A7X2_9FLAO
LinkDB: A0A1M6A7X2_9FLAO
Original site: A0A1M6A7X2_9FLAO 
ID   A0A1M6A7X2_9FLAO        Unreviewed;       871 AA.
AC   A0A1M6A7X2;
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=SAMN04488096_101129 {ECO:0000313|EMBL:SHI32568.1};
OS   Mesonia phycicola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mesonia.
OX   NCBI_TaxID=579105 {ECO:0000313|EMBL:SHI32568.1, ECO:0000313|Proteomes:UP000184225};
RN   [1] {ECO:0000313|EMBL:SHI32568.1, ECO:0000313|Proteomes:UP000184225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21425 {ECO:0000313|EMBL:SHI32568.1,
RC   ECO:0000313|Proteomes:UP000184225};
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; FQYY01000001; SHI32568.1; -; Genomic_DNA.
DR   RefSeq; WP_073147190.1; NZ_FQYY01000001.1.
DR   AlphaFoldDB; A0A1M6A7X2; -.
DR   STRING; 579105.SAMN04488096_101129; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000184225; 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:SHI32568.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHI32568.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184225};
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          410..528
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   871 AA;  97765 MW;  F8A0E1F716A5B602 CRC64;
     MNLNNYTIKS QEAIQQAQQL AQEYGHQQIE NEHIFKAITS IDENVTPFLL KKLNINVGLF
     TQIVDKTLES FPKVSGGDIV LSREAGKMLN DASTIAKKMN DEYVSIEHLI LAIFNSKSKV
     AQILKDQGAT EKGLKAAIEE LRKGDRVTSQ SAEETYNSLN KFAKNLNQLA ESGKLDPVIG
     RDEEIRRILQ ILSRRTKNNP MLVGEPGTGK TAIAEGLAHR IVAGDVPENL KNKEIFSLDM
     GALIAGAKYK GEFEERLKAV IKEVTSSDGN IVLFIDEIHT LVGAGGGQGA MDAANILKPA
     LARGELRAIG ATTLDEYQKY FEKDKALERR FQRVTVDEPD TESAISILRG IKEKYETHHK
     VRIKDEAIIS AVELSQRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
     EIEIEAIKRE KDEVKLKSLK SDLANLKEER AELNAQWQNE KGVVDNIQQA KTDIENYKLE
     AERAERDGDY GKVAELRYGK IKEAQQNLEK LQKEVEEQKH EGKKSLIQEE VTSDDIAEVV
     AKWTGIPVTK MLQSEREKLL KLEDELHKRV VGQEEAIQAV SDAIRRSRAG LQDQKKPIGS
     FLFLGTTGVG KTELAKALAE YLFDDDNAMT RIDMSEYQER HSVSRLVGAP PGYVGYDEGG
     QLTEAVRRKP YSVVLLDEIE KAHPDTFNIL LQVLDEGRLT DNKGRLADFR NTIIIMTSNM
     GSHIIQEKFD AIPDVETAME GAKVEVLGLL KQQVRPEFLN RIDDIVMFTP LTQENISEIV
     GLQLKGITKM LSEQHITLDA TPEAIKFLAK QGFDPQYGAR PVKRTLQKEV LNTLSKEILS
     GEVTTDSIIL LDAFNDKLVF RNETNNVLDT H
//
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