ID G2EFL5_9FLAO Unreviewed; 867 AA.
AC G2EFL5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:EGV42741.1};
GN ORFNames=BZARG_2497 {ECO:0000313|EMBL:EGV42741.1};
OS Bizionia argentinensis JUB59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Bizionia.
OX NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV42741.1, ECO:0000313|Proteomes:UP000003730};
RN [1] {ECO:0000313|EMBL:EGV42741.1, ECO:0000313|Proteomes:UP000003730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUB59 {ECO:0000313|EMBL:EGV42741.1,
RC ECO:0000313|Proteomes:UP000003730};
RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0;
RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M.,
RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., Criscuolo M.,
RA Memoli M., Arguelles M., Mac Cormack W.P.;
RT "Bizionia argentinensis sp. nov., isolated from surface marine water in
RT Antarctica.";
RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008).
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:EGV42741.1}.
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DR EMBL; AFXZ01000044; EGV42741.1; -; Genomic_DNA.
DR RefSeq; WP_008638558.1; NZ_AFXZ01000044.1.
DR AlphaFoldDB; G2EFL5; -.
DR STRING; 1046627.BZARG_2497; -.
DR PATRIC; fig|1046627.3.peg.2300; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000003730; 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 78, MITOCHONDRIAL; 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:UP000003730};
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 867 AA; 97468 MW; ADDF3D0BB86AB71C CRC64;
MNFNNYTIKS QEAIQQAQQL AQSFGHQQIE NEHIFKALFN VDENVLPFIL KKLNVNISIL
QQTLDKQLES FPKVSGGEIM LSREANKSLN EAAIIAKKMT DEYVSIEHLI LAIFKSNSKI
SQMLKDQGVT EKHLKAAIDE LRQGDRVTSQ SQEETYNSLN KYAKNLNQLA KDGKLDPVIG
RDEEIRRILQ ILSRRTKNNP ILVGEPGTGK TAIAEGLAHR IVDGDIPENL IDKQIFALDM
GALIAGAKYK GEFEERLKAV IKEVTESDGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEQDKALERR FQKVMVDEPD TESAISILRG IKEKYETHHK
VRIKDEAIIG AVELSERYIT NRFLPDKAID LMDEAAAKLR MEINSKPEEL DVLDRKVMQL
EIEIEAIKRE KDESKLKSLR ADLANLKEDR NELNAKWKSE KEVVDNIQNA KSNIEEFKLE
AERAERDGDY GKVAEIRYGK IQEAQERLEN LQKELAANQS ESSLIKEEVT YEDIADVVAK
WTGIPISKML QTDREKLLKL EDELHKRVVG QNEAIIAVSD AVRRSRAGLQ NPQKPIGSFL
FLGTTGVGKT ELAKALAEYL FDDEAAMTRI DMSEYQERHA VSRLIGAPPG YVGYDEGGQL
TEAVRRKPYS VVLLDEIEKA HPDTFNILLQ VLDEGHLTDN KGRLADFKNT IIIMTSNMGS
QIIQEKFEAT KDVDAAMELA KIEVLGLLKQ TVRPEFLNRI DDTIMFTPLT KDNITEIVGL
QLKSITKMIG KQGITFDATP EAVSYLAQKG YNPEYGARPV KRVIQKEVLN ELSKEILSGN
VSTDSIILLD AFDDHLVFRN QGDLVKE
//
