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Database: UniProt
Entry: A0A5J4FWQ2_9FLAO
LinkDB: A0A5J4FWQ2_9FLAO
Original site: A0A5J4FWQ2_9FLAO 
ID   A0A5J4FWQ2_9FLAO        Unreviewed;       867 AA.
AC   A0A5J4FWQ2;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   13-SEP-2023, entry version 13.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:GEQ86630.1};
GN   ORFNames=ULMS_21380 {ECO:0000313|EMBL:GEQ86630.1};
OS   Patiriisocius marinistellae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Patiriisocius.
OX   NCBI_TaxID=2494560 {ECO:0000313|EMBL:GEQ86630.1, ECO:0000313|Proteomes:UP000326994};
RN   [1] {ECO:0000313|EMBL:GEQ86630.1, ECO:0000313|Proteomes:UP000326994}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KK4 {ECO:0000313|EMBL:GEQ86630.1,
RC   ECO:0000313|Proteomes:UP000326994};
RA   Kawano K., Ushijima N., Kihara M., Itoh H.;
RT   "Ulvibacter marinistellae sp. nov., isolated from a starfish, Patiria
RT   pectinifera.";
RL   Submitted (AUG-2019) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GEQ86630.1}.
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DR   EMBL; BKCF01000004; GEQ86630.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5J4FWQ2; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000326994; 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: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 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000326994};
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..521
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   867 AA;  97372 MW;  18BA799FE5597309 CRC64;
     MNFNNYTIKS QEAIQQAQQL AQGYGHQQIE NEHIMKAIFE VDENVTPFLL KKLNVNVSTL
     QQILDKQLES FPKVSGGDIM LSRSASSTVN EASNIAKKMN DEYVSVEHLL LAIFKSKSNI
     AQTLKDQGVT EKGLKAAIEE LRKGDRVTSQ SAEETYNSLN KYARNLNQLA RDGKLDPVIG
     RDEEIRRILQ ILTRRTKNNP MLVGEPGTGK TAIAEGLAHR IVDGDVPENL KTKEVFSLDM
     GALIAGAKFK GEFEERLKAV IKEVTSSDGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
     LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVMVNEPD TESAISILRG IKEKYEAHHK
     VRIKDEAIIA AVELSQRYIT NRFLPDKAID LMDEAASKMR MEINSKPEEL DVLDRKVMQL
     EIEIEAIKRE NDETKLKSLR SDLANIKEER NELNAKWKSE KEVVENVQNL KTEIEDYKLE
     AERAEREGDF GKVAEIRYGK IKETQEKLSE LEQQLAKNQS GNSLIKEEVT NEDIAEVVAK
     WTGIPVTKML QSDREKLLKL ENELHKRVVG QEEAIVAVSD AVRRSRAGLQ DPKKPLGSFL
     FLGTTGVGKT ELAKALAAYM FDDDNAMTRI DMSEYQERHS VSRLVGAPPG YVGYDEGGQL
     TEAVRRKPYS VVLLDEIEKA HPDTFNILLQ VLDEGRLTDN KGRIADFKNT IIIMTSNMGS
     EIIQQKFETV KDPETAMEGA KVEVLGLLKQ MVRPEFLNRI DDIIMFTPLN KDHIKKIVGL
     QLKGLSKMLT KQGITLDATD EAINYLSEKG FDPQFGARPV KRVIQKEVLN ELSKEILSGK
     VTTDSIILLD SFDSKLVFRN QNDLVTN
//
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