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Database: UniProt
Entry: A0A3S9P7N7_9BACT
LinkDB: A0A3S9P7N7_9BACT
Original site: A0A3S9P7N7_9BACT 
ID   A0A3S9P7N7_9BACT        Unreviewed;       869 AA.
AC   A0A3S9P7N7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:AZQ64219.1};
GN   ORFNames=EI427_18895 {ECO:0000313|EMBL:AZQ64219.1};
OS   Flammeovirga pectinis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Flammeovirga.
OX   NCBI_TaxID=2494373 {ECO:0000313|EMBL:AZQ64219.1, ECO:0000313|Proteomes:UP000267268};
RN   [1] {ECO:0000313|EMBL:AZQ64219.1, ECO:0000313|Proteomes:UP000267268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L12M1 {ECO:0000313|EMBL:AZQ64219.1,
RC   ECO:0000313|Proteomes:UP000267268};
RA   Bae J.-W., Jeong Y.-S., Kang W.;
RT   "Flammeovirga pectinis sp. nov., isolated from the gut of the Korean
RT   scallop, Patinopecten yessoensis.";
RL   Submitted (DEC-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}.
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DR   EMBL; CP034562; AZQ64219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S9P7N7; -.
DR   KEGG; fll:EI427_18895; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000267268; Chromosome 1.
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:UP000267268};
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          411..522
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   869 AA;  97739 MW;  3FDDF2D62B6375A3 CRC64;
     MNFEKYTIRS QEVLQKAQNI AKGLQQQIIE TGHILKAIIQ QEDNMITFLT NKIKADKATL
     DTQVDTIVNT YSKSSGENPY LSNDSANTLQ KAEQFMADMG DEFVAVEHIL LGLLDGNDKI
     ASLLKQAGFT NDYLKKAIVE LRKGNKVTDQ NAEGQYQSLE RYAVDLTQMA RDGKLDPVIG
     RDEEIRRVLQ ILSRRTKNNP MLIGEPGVGK TAIAEGLAQR IVSGDIPENL EDISIASLDM
     GALVAGAKFK GEFEERLKAV IKEVQSAEGK IILFIDEIHT LIGAGAGGDS AMDAANLLKP
     ALARGELRSI GATTLKEYQK YIEKDKALER RFQPVKVGEP SVDDAISILR GIKEKYEVHH
     GVRIKDDAII SSVELSNRYI SDRFLPDKAI DLMDEAAARM RIQMNSMPEE VDEIKRKVMQ
     LEIEREAIRR EEDVEKENIL TDQIRILTGK LNELEDEWKR EKQTLDGIKQ LKRDIDKYKI
     EADQAERSGN YGRVAEIRYG KIVEAEKQLE DLQKESEIES ESGNVMLRQE VTSDDIAEVV
     ARWTGIPVAK MVQGEREKLL HLETELGNRV AGQDEAIVAI SDAVRRSRAG LQDPRRPIGS
     FLFLGTTGVG KTELAKALAD YLFDDEKAMV RIDMSEYQEK HAVSRLIGAP PGYVGYDEGG
     QLTEEVRRRP YSVILLDEIE KAHPDVFNIL LQVLDDGRLT DNKGRVADFK NTIVIMTSNM
     GAHFMMDKIG DLEKAETVLE KDEILEGCKV QALDLLKNTV RPEFLNRIDE ICMFQPLTRE
     NMGKIASIQF KDIQKRIRAN GIEIEITPEA LKKVADLGYE PEFGARPLKR VIQRYILNDL
     SKSILSGKVE KDSIVLIDIE NDQLVFKNK
//
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