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Database: UniProt
Entry: A0A099KE01_9GAMM
LinkDB: A0A099KE01_9GAMM
Original site: A0A099KE01_9GAMM 
ID   A0A099KE01_9GAMM        Unreviewed;       857 AA.
AC   A0A099KE01;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=ND16A_0187 {ECO:0000313|EMBL:KGJ88247.1};
OS   Thalassotalea sp. ND16A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGJ88247.1, ECO:0000313|Proteomes:UP000029848};
RN   [1] {ECO:0000313|EMBL:KGJ88247.1, ECO:0000313|Proteomes:UP000029848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND16A {ECO:0000313|EMBL:KGJ88247.1,
RC   ECO:0000313|Proteomes:UP000029848};
RA   Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA   Hazen T.C.;
RT   "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT   Eastern Mediterranean Deep Water.";
RL   Submitted (AUG-2014) 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:KGJ88247.1}.
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DR   EMBL; JQDZ01000119; KGJ88247.1; -; Genomic_DNA.
DR   RefSeq; WP_033079133.1; NZ_JQDZ01000119.1.
DR   AlphaFoldDB; A0A099KE01; -.
DR   STRING; 1535422.ND16A_0187; -.
DR   PATRIC; fig|1535422.3.peg.3630; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000029848; 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:UP000029848};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   857 AA;  95112 MW;  6BD4B1AEAEF5F158 CRC64;
     MRIDKLTQKF QQALADAQSL ALGKDNQFIE PTHLMLALLN QSGGSVLPIL KSCAVDISSL
     RTKITQMLEQ LPQVEGVGGE IQVSTQLASL LNLCDKLAQK QQDKFISSEM FLLAALQDKG
     PLGQLLKTLA IKEKQIKQAI EKARGGQTVD DPNAEDTRQA LDKYTVNLTE SAEQGKLDPV
     IGRDEEIRRT LQVLQRRTKN NPVLIGQPGV GKTAIVEGLA QRIINGEVPE GLKNKQVLSL
     DMGALIAGAK YRGEFEERLK AVLNELAKEE GEIILFIDEL HTMVGAGKSD GAMDASNMLK
     PALARGDLHC VGATTLDEYR QYIEKDAALE RRFQKVLVEE PSVADTIAIL RGLKERYELH
     HKVDITDPAI VSAASLSHRY ISDRQLPDKA IDLIDEAASS IRMQMDSKPE DLDRLERRLI
     QLKLEQKAVE KETDAASQKR LKLMEEEINN IQGRYDQLEQ VWKQEKASLY GAQTIKADIE
     QARLDLEVAQ RAGDLNRMSE LQYGRIPELE KQLEHAANAD AVDLKLLKNK VTDVEIAEVL
     SKATGIPVAK MLEGERDKLL HMELDLKKQV IGQSQALTAV SNAIRRSRAG LSDPNQPIGS
     FMFLGPTGVG KTELTKALAK FLFDSEQALI RVDMSEFMEK HSVARLIGAP PGYVGYEEGG
     YITEAVRRKP YSVILLDEIE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVIIMTSNM
     GSDIIQEMAG ESHYEQMRDT VMAVVAQHFK PEFINRIDES VVFHPLNAEQ IQQIASIQIK
     ILAGRLAEKQ LSLEISDDAL AKVSESGFDP VFGARPLKRA IQRNIENPLA QELLAGKYLP
     ESTITIDVDS EGKLMIN
//
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