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
//