ID A0A0Q4ELN7_9FLAO Unreviewed; 864 AA.
AC A0A0Q4ELN7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ASE55_09095 {ECO:0000313|EMBL:KQM50244.1};
OS Chryseobacterium sp. Leaf201.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1735672 {ECO:0000313|EMBL:KQM50244.1, ECO:0000313|Proteomes:UP000051097};
RN [1] {ECO:0000313|EMBL:KQM50244.1, ECO:0000313|Proteomes:UP000051097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf201 {ECO:0000313|EMBL:KQM50244.1,
RC ECO:0000313|Proteomes:UP000051097};
RX PubMed=26633631; DOI=10.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf201 {ECO:0000313|Proteomes:UP000051097};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf201 {ECO:0000313|Proteomes:UP000051097};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQM50244.1}.
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DR EMBL; LMKA01000054; KQM50244.1; -; Genomic_DNA.
DR RefSeq; WP_056216313.1; NZ_LMKA01000054.1.
DR AlphaFoldDB; A0A0Q4ELN7; -.
DR STRING; 1735672.ASE55_09095; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051097; 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 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 864 AA; 97507 MW; 3B5AD5E5F1260409 CRC64;
MNLNQYTVKS QEAIQAAQQV AMEFGNQSIE PQHLLEGIFQ VDENISPFLL KKSEADAALV
RERNRENLEK LPKVQGGNIY LSQSANKVLL DAPNIAKKMG DEFVTIEHLW LSLLETNSEV
SKMLKDMGMT RSLLEGGIKE LRKGSKATSA SSEETYQSLN KYAKNFNELA AEGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP ILIGEPGVGK TAIAEGIAHR IISGDIPENL MDKTLYSLDM
GALIAGAKYK GEFEERLKSV INEVTKSNGQ IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLNEYQKY FEKDKALERR FQKVTVEEPD TESAISILRG IKDKYEAHHK
VRIKDEAIIA AVEMSQRYIS DRFLPDKAID LIDEASAKLR MEINSKPEEL DVLDRKLMQM
EIELAAISRE GNQTKIEHLK EDISKISEQR NEINAKWLKE KQKSEDLTSI KKDIESLKLE
AERASRAGDY AKVAEIQYGK IKEKEDALQK LELEMQNHQN ELIKEEVTSE NISEVIAKWT
GIPVTKLLQS EREKLLHLEN EIHHRVVGQD EAIQAVADAI RRNRAGLSDE KKPIGSFLFL
GTTGVGKTEL AKALAEFLFD DENNMTRIDM SEYQERHSVS RLVGAPPGYV GYDEGGQLTE
AVRRRPYSVV LLDEIEKAHP DVFNTLLQVL DDGRLTDNKG RVVNFKNSII IMTSNLGSHL
IQENFENITD ENQDEIVDKT KEEVFDLLKQ TLRPEFLNRI DEIVLFQPLR KKEIGKIVTY
QLRGFNDMLA KRNIIMTATQ DALNYLTNKG YDPAFGARPL KRVIQQEVLN KLSREILAGT
VNDGDRITLD YFEETGLVFR PAEL
//