ID A0A3M8GHS1_9FLAO Unreviewed; 866 AA.
AC A0A3M8GHS1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-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:RNC89867.1};
GN ORFNames=ED555_10465 {ECO:0000313|EMBL:RNC89867.1};
OS Allomuricauda sp.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=192149 {ECO:0000313|EMBL:RNC89867.1, ECO:0000313|Proteomes:UP000280438};
RN [1] {ECO:0000313|EMBL:RNC89867.1, ECO:0000313|Proteomes:UP000280438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin2 {ECO:0000313|EMBL:RNC89867.1};
RA Zheng Q., Wang Y., Jiao N.;
RT "Metagenomics and metaproteomics analyze the interactions between
RT Synechococcus and associated heterotrophic bacteria in one oligotrophic
RT Synechococcus culture.";
RL Submitted (OCT-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:RNC89867.1}.
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DR EMBL; RHLF01000002; RNC89867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8GHS1; -.
DR Proteomes; UP000280438; 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 78, MITOCHONDRIAL; 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:UP000280438};
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 866 AA; 97251 MW; 12C0876E62FF575B CRC64;
MNLNNFTIKS QEAIRQAQLL AQELGHQQIE NEHVYKAIGI VDENVLPFIL KKLAVNAEMV
QQILENELES LPKVSGGDFM FSREAGKTLN EATLVAKKMN DEFVSLEHLL LAIFKSKSKI
SQILKDQGAT EKALIAAIEE LRKGNRVTSQ SAEETYNALS KYANNLNAMA DSGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP MLVGEPGVGK TAIAEGLAHR IVQGDVPENL KEKTIFSLDM
GALIAGAKYK GEFEERLKSV IKEVTTSDGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
LARGALRAIG ATTLDEYQKY FEKDKALERR FQKVVVDEPD TESAISILRG IKEKYETHHK
VRIKDEAVIA AVELSQRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
EIEIEAIKRE NDKEKLKALN LELANLKEER NQIFAKWESE KSLVDGIQKT KQDIENFKQE
AERAERNGDY GKVAELRYGK IKEAQEKLET LQDQLLAEQS SETLIKEEVT NDDIAEVVAK
WTGIPVTKMM QSEREKLLQL EQVMEKRVVG QEEAIEAVSD AIRRSRAGLQ DSRRPIGSFL
FLGTTGVGKT ELAKTLAAYL FDDENALTRI DMSEYQERHS VSRLVGAPPG YVGYDEGGQL
TEAVRRKPYS VILLDEIEKA HPDTFNILLQ VLDEGRLTDN KGRVADFKNA IIIMTSNLGS
HIIQEQFEAS DNIENAIASS RAEVLGLLKK TVRPEFLNRI DDIVMFTPLN KSDIKEIVKL
QLEQLKKLVA KQHITLDATE EAIDYLSNKG YDPQYGARPI KRLIQKEVLN NLSKELLAGR
LKNESIVLLD SFDNALVFRN HSELVN
//
