ID A0A238UAE5_9FLAO Unreviewed; 867 AA.
AC A0A238UAE5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:SNR15956.1};
GN ORFNames=TJEJU_2270 {ECO:0000313|EMBL:SNR15956.1};
OS Tenacibaculum jejuense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=584609 {ECO:0000313|EMBL:SNR15956.1, ECO:0000313|Proteomes:UP000215214};
RN [1] {ECO:0000313|EMBL:SNR15956.1, ECO:0000313|Proteomes:UP000215214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=type strain: KCTC 22618 {ECO:0000313|Proteomes:UP000215214};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) 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}.
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DR EMBL; LT899436; SNR15956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238UAE5; -.
DR KEGG; tje:TJEJU_2270; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000215214; Chromosome tjeju.
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:UP000215214};
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; 97790 MW; D57B86B0BC192C10 CRC64;
MNFNNFTIKS QETVQLAQQI TQEYSHNQIE NEHFFKALLQ VDKNVLPYIL KKLNVNVDLV
SQVLEKQLQS FSKVNGVDIM LSREANKTLN EASIIAKKMN DEYVSVEHLI LAIFSSKSQI
AQFLKDQGVN EKNLKAAIEE LRKGNRVTSQ SAEESYNALN KYAKNLNQLA QDGKLDPVIG
RDEEIRRLLQ ILSRRTKNNP ILVGEPGTGK TAIAEGLAHR IIKGDVPENL KDKEIYSLDM
GALIAGAKFK GEFEERLKAV VKEVTSSEGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVMVDEPD TESAISILRG IKEKYETHHK
VRIKDEAIIG AVELSQRYIT SRFLPDKAID LMDEAAAKLR MEINSKPEEL DVLDRKIMQL
EIEIEAIKRE NDDLKLKSLN ADLANLKEER NDINAKWQSE KSVVDTIQKL KTDIEDYKLE
AEKAERNGDY GRVAELRYGK IKEAQEALEQ QQETLINESD NTLIKEEVTY DDIAEVVAKW
TGIPVTKMLQ SEREKLLRLE DELHKRVVGQ EEAIEAVSDA VRRSRAGLQN PNKPIGSFLF
LGTTGVGKTE LAKALASYLF DDENAMTRID MSEYQERHSV SRLVGAPPGY IGYDEGGQLT
EAVRRKPYSV VLLDEIEKAH PDTFNILLQV LDEGRLTDNK GRVADFKNTI IIMTSNMGSH
IIQEKYETMN GAIEASMDLA KEEVLGLLKQ SVRPEFLNRI DDIIMFTPLS KDNIKSIVRL
QLNHIKKMIS AQNITLDATE QAITHLAEKG FQPEFGARPV KRVIQKQVLN LLSKEILAGK
ISNDSLILLD EFDGTLVFRN PIHDEEE
//