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Database: UniProt
Entry: A0A5B1BF55_9FLAO
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ID   A0A5B1BF55_9FLAO        Unreviewed;       866 AA.
AC   A0A5B1BF55;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   13-SEP-2023, entry version 13.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:KAA1247036.1};
GN   ORFNames=F0000_04950 {ECO:0000313|EMBL:KAA1247036.1};
OS   Aquimarina sp. RZ0.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aquimarina.
OX   NCBI_TaxID=2607730 {ECO:0000313|EMBL:KAA1247036.1, ECO:0000313|Proteomes:UP000323420};
RN   [1] {ECO:0000313|EMBL:KAA1247036.1, ECO:0000313|Proteomes:UP000323420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RZ0 {ECO:0000313|EMBL:KAA1247036.1,
RC   ECO:0000313|Proteomes:UP000323420};
RA   Chen X.-Y.;
RL   Submitted (SEP-2019) 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:KAA1247036.1}.
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DR   EMBL; VTZU01000008; KAA1247036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5B1BF55; -.
DR   Proteomes; UP000323420; 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   Reference proteome {ECO:0000313|Proteomes:UP000323420};
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   866 AA;  97298 MW;  AA453286541037D1 CRC64;
     MNFNNFTIKS QETIQQAQEL AQSFGHQQIE NEHIFKAIFT VDESVLPFLL KKLNVNISLL
     QQVLDSTLDS FPKVSGGELQ LSRDVGTTLN EASIIAKKMN DEYVSIEHLI LAIFKSKSKI
     AQILKDQGVT QKHLTEAITE IRKGERVTSQ NAEDTYQSLN KYAKNLNELA ENGKLDPVIG
     RDEEIRRILQ ILSRRTKNNP MLVGEPGVGK TAIAEGLAHR IIAGDIPDNL KDKQIYSLDM
     GALIAGAKFK GEFEERLKAV VKEVTSSDGN IVLFIDEIHT LVGAGGGQGA MDAANILKPA
     LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVMVDEPD TESAISILRG IKEKYETHHK
     VRIKDEAIIA AVELSQRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
     EIEIEAIKRE NDETKLKSLN ADLANFKEER NEIFAKWQSE KEVVDAIQNA KTSIETYKQE
     AERAERNGEY GKVAELRYGK IKDVQEQLET LQEQLDQQQN ASSLIKEEVT NDDIAEVVAK
     WTGIPVTKML QSEREKLLVL EKELQKRVVG QSEAILAVSD AVRRSRAGLQ DQKKPIGSFL
     FLGTTGVGKT ELAKALADYL FDDETAMTRI DMSEYQERHS VSRLVGAPPG YIGYDEGGQL
     TEAVRRKPYS VVLLDEIEKA HPDTFNILLQ VLDEGRLTDN KGRVADFRNT IIIMTSNLGG
     HIIQDKFKAV DNVDAAMESA KVEVLGLLKQ SVRPEFLNRI DDIIVFTPLT RGNINEIVKL
     QLKQVSRMLS KQHITLDATN EAIDFLAERG YQPEFGARPV KRTIQKEVLN ALSKEILAGN
     VSTDSIILLD EFDNNLVFRN QTDLVT
//
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