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Database: UniProt
Entry: A0A2T1NH73_9FLAO
LinkDB: A0A2T1NH73_9FLAO
Original site: A0A2T1NH73_9FLAO 
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}.
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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
//
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