ID A0A099Y267_9FLAO Unreviewed; 869 AA.
AC A0A099Y267;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=PHEL85_0629 {ECO:0000313|EMBL:KGL63592.1};
OS Polaribacter sp. Hel1_85.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL63592.1, ECO:0000313|Proteomes:UP000029991};
RN [1] {ECO:0000313|EMBL:KGL63592.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL63592.1};
RA Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T.,
RA Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., Teeling H.;
RT "Niches of two polysaccharide-degrading Polaribacter strains isolated from
RT the North Sea during a spring diatom bloom.";
RL ISME J. 0:0-0(2014).
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:KGL63592.1}.
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DR EMBL; JPDS01000001; KGL63592.1; -; Genomic_DNA.
DR RefSeq; WP_036820890.1; NZ_JPDS01000001.1.
DR AlphaFoldDB; A0A099Y267; -.
DR STRING; 1250005.PHEL85_0629; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000029991; 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 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 869 AA; 97867 MW; 4A65E6FB068C1B97 CRC64;
MNFNNYTTKS QETIQMAQQI AQGFGHNQIE NEHIFKALTQ VDENVLPFLL KKLNINLNIV
EQILDKQLES LPKVSGAELM LSREASKTLT EAAVIAKKMK DDYVSIEHLI LAIFKSKSNI
AQVLKDQGVT EKHLQAAIEE LRKGEKVTSQ NQEETYNSLN KYAKNLNQLA EDGKLDPVIG
RDEEIRRLLQ ILSRRTKNNP LLVGEPGTGK TAIAEGLAHR IVDGDVPENL KDKLIFSLDM
GALIAGAKYK GEFEERLKAV IKEVTSSDGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVQVNEPD TESAISILRG IKDKYETHHK
VRIKDEAIIG AVELSQRYIT NRFLPDKAID LMDEAMAKLR MEINSKPEEL DVLDRKVMQL
EIEIEAIKRE KDEVKLKALR SDLANLKEER NEMNAKWKSE KEVVDNIQNA KAAIEDFKME
AEKAEREGDY GKVAEIRYGK IKKAEEDLEE LQNALKENQS ETSLIKEEVT YDDIAEVVAK
WTGVPVTKMI QSEREKLLRL ESQLHKRVVG QEEAIVAVSD AVRRSRAGLQ NPNKPIGSFL
FLGTTGVGKT ELAKALAEYM FDDENAMTRI DMSEYQEKHS VSRLVGAPPG YVGYDEGGQL
TEAVRRRPYS VVLLDEIEKA HPDTFNVLLQ VLDEGRLTDN KGRVADFKNT IIIMTSNMGS
HIIQEKFDNL KGDVETTMEL AKVEVLGLLK QSVRPEFLNR IDDIIMFAPL SKENIQEIVR
IQLNSVKKMA AEQNITLDAT DEAINYLAIK GYQPEFGARP VKRVIQKEVL NQLSKEILSG
KVTTDSIVLL DAFDDKLVFR NQSDLVENE
//
