ID A0A086F7W3_CHRP1 Unreviewed; 863 AA.
AC A0A086F7W3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=HX13_08830 {ECO:0000313|EMBL:KFF75027.1};
OS Chryseobacterium sp. (strain P1-3).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1517683 {ECO:0000313|EMBL:KFF75027.1, ECO:0000313|Proteomes:UP000028723};
RN [1] {ECO:0000313|EMBL:KFF75027.1, ECO:0000313|Proteomes:UP000028723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-3 {ECO:0000313|EMBL:KFF75027.1,
RC ECO:0000313|Proteomes:UP000028723};
RA Park G.-S., Hong S.-J., Kwak Y., Choi J.-B., Jung B.K., Lee C.H.,
RA Shin J.-H.;
RT "Chryseobacterium sp. P1-3 whole genome sequence.";
RL Submitted (JUL-2014) 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:KFF75027.1}.
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DR EMBL; JPEQ01000006; KFF75027.1; -; Genomic_DNA.
DR RefSeq; WP_050020706.1; NZ_JPEQ01000006.1.
DR AlphaFoldDB; A0A086F7W3; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000028723; 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:KFF75027.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KFF75027.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028723};
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 863 AA; 97476 MW; 700D177B97268E1E CRC64;
MNLNQYTVKS QEAIQAAQQV AMEFGNQSIE PQHLLEGIFQ VDENISPFLL KKSEADASLV
RERNRESIEK LPKVQGGNIY LSQSANKVLL DAPNIAKKMG DEFVTIEHLW LSLLETSSEV
SKMLKDMGVT KNLLEGAIKE LRKGSKATSA SSEETYQSLN KYAKNFNELA AEGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP ILIGEPGVGK TAIAEGIAHR IISGDVPENL MDKTLYSLDM
GALIAGAKYK GEFEERLKSV VNEVIKSDGQ IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLNEYQKY FEKDKALERR FQKVMVEEPD TESAISILRG IKDKYEAHHK
VRIKDEAIIA AVEMSQRYIS DRFLPDKAID LIDEASAKLR MEINSKPEEL DVLDRKLMQM
EIELAAISRE GNQTKIDHLK EDIAKISEQR NEINAKWLKE KQKSEDLTQI KKEIESLKLE
AERASRAGDY AKVAEIQYGK LREKEEELSK VELEMQNHQN ELIKEEVTAE NISEVIAKWT
GIPVTKLLQS EREKLLNLES ELHHRVVGQD EAIQAVADAI RRNRAGLSDD KKPIGSFLFL
GTTGVGKTEL AKALAEFLFD DENNMTRIDM SEYQERHSVS RLVGAPPGYV GYDEGGQLTE
AVRRRPYSVV LLDEIEKAHP DVFNTLLQVL DDGRLTDNKG RVVNFKNSII IMTSNLGSHL
IQENFENITD ANQDEIVDKT KEEVFDLLKQ TLRPEFLNRI DEIVLFQPLR KKEIGKIVQY
QLRGFNDMLA KRNIIMTFTQ DAVDYLMEKG YDPVFGARPL KRVIQQDVLN KLSREILAGK
VNDGDRITLD YFDETGLVFR PTE
//