ID A0A2T1NH73_9FLAO Unreviewed; 868 AA.
AC A0A2T1NH73;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PSG92185.1};
GN ORFNames=C7H61_06310 {ECO:0000313|EMBL:PSG92185.1};
OS Mesoflavibacter zeaxanthinifaciens subsp. sabulilitoris.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Mesoflavibacter.
OX NCBI_TaxID=1520893 {ECO:0000313|EMBL:PSG92185.1, ECO:0000313|Proteomes:UP000238430};
RN [1] {ECO:0000313|EMBL:PSG92185.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42117 {ECO:0000313|EMBL:PSG92185.1};
RA Cheng H., Wu Y.-H., Guo L.-L., Xu X.-W.;
RT "Mesoflavibacter sp. HG37 and Mesoflavibacter sp. HG96 sp.nov., two marine
RT bacteria isolated from seawater of Western Pacific Ocean.";
RL Submitted (MAR-2018) 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:PSG92185.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PXOT01000020; PSG92185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1NH73; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000238430; 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..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 97544 MW; 75CEA5E110DD16C4 CRC64;
MNLNNYTIKS QEAIQQSQQI AQSYGHQQIE NEHLFKGILE VDENVLPFLL KKLNVNTIVL
KQALDKQLES FAKVSGADLM LSREAGKTLN EASIIAKNMK DDFVSVEHLI LAILKSNSKI
AQMLKDQSVT EKGLKAAIEE LRKGDRVTSQ SQEDTYNSLN KYAKNLNQLA KDGKLDPVIG
RDEEIRRILQ ILSRRTKNNP ILVGEPGTGK TAIAEGLAHR IVDGDVPENL KEKQIFALDM
GALIAGAKFK GEFEERLKAV IKEVTTSEGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
LARGELRSIG ATTLDEYQKY FEKDKALERR FQKVMVDEPD TESAISILRG IKEKYETHHK
VRIKDEAIIG AVELSQRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
EIEIEAIKRE KDEVKLKSLR SDLANLKEER NEINAKWKSE KEVVDNIQNT KQDIENFKLE
AERAEREGNY GKVAELRYGK IKEAQEKLES LQKDLQSQSE HSLIKEEVNY DDIAEVVAKW
TGIPVTKMLQ SEREKLLKLE DELHKRVVGQ EEAIEAVSDA VRRSRAGLQN PQKPIGTFLF
LGTTGVGKTE LAKALAEYLF DDENAMTRID MSEYQERHAV SRLVGAPPGY VGYDEGGQLT
EAVRRKPYSV VLLDEIEKAH PDTFNILLQV LDEGHLTDNK GRMADFKNTI IIMTSNMGSH
IIQERFEATK DVESAMEAAK VDVLGLLKQT VRPEFLNRID DTIMFTPLTQ DNITQIVGLQ
LKSVTKMIAK QGITFDATPE AIAYLAEKGY NPEYGARPVK RVIQKEVLNQ LSKEILAGKI
NTDSIILLDA FDGELVFRNQ GDLVEGEL
//