GenomeNet

Database: UniProt
Entry: A0A251WB88_9CYAN
LinkDB: A0A251WB88_9CYAN
Original site: A0A251WB88_9CYAN 
ID   A0A251WB88_9CYAN        Unreviewed;       874 AA.
AC   A0A251WB88;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=B0A82_20095 {ECO:0000313|EMBL:OUC12860.1};
OS   Alkalinema sp. CACIAM 70d.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Alkalinema.
OX   NCBI_TaxID=1934309 {ECO:0000313|EMBL:OUC12860.1, ECO:0000313|Proteomes:UP000194922};
RN   [1] {ECO:0000313|EMBL:OUC12860.1, ECO:0000313|Proteomes:UP000194922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CACIAM 70d {ECO:0000313|EMBL:OUC12860.1};
RA   Lima A.R., Siqueira A.S., Pereira J.S., Goncalves E.C.;
RT   "Draft genome of Alkalinema sp. CACIAM 70d.";
RL   Submitted (JAN-2017) 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|ARBA:ARBA00004496,
CC       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:OUC12860.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MUGG01000168; OUC12860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251WB88; -.
DR   STRING; 1934309.B0A82_20095; -.
DR   Proteomes; UP000194922; 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:UP000194922};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          6..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          414..528
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   874 AA;  98315 MW;  C13770FF978E7F32 CRC64;
     MQPSNPNQFT EKAWEAIGRT PDIVKQANQQ QIETEHLMKA LLEQDGLAAS VFNKLGVSVQ
     RLRDRTEEYI AKQPKVSGAN QNVYFGRSSD SLLDRAESYR KQYGDDFISV EHMLLGYAQD
     SRFGKALFAE FKLDEAKLKA AIEQIRGNQK VTDQNPEGKY EVLEKYGRDL TKYAKEGKLD
     PVIGRDDEIR RTIQILSRRT KNNPVLIGEP GVGKTAIAEG LAQRIVSGDV PQSLKDRTLI
     ALDMGALIAG AKYRGEFEER LKAVLKEVTD SQGNIILFID EIHTVVGAGA TQGAMDAGNL
     LKPMLARGEL RCIGATTLDE YRKYIEKDAA LERRFQQVYV DQPSVEDTIS ILRGLKERYE
     LHHGVKISDS SLVAAATLST RYISDRFLPD KAIDLVDEAA AKLKMEITSK PEQLDEVDRK
     ILQLEMERLS LQKESDVASK ERLQRLEKEL ADLKEEQSRL NAQWQAEKGG IGELQKIKEE
     IDRVNLEVQQ AERDYDLNRA AELKYGTLAQ LQKKLEATEA KLTATQTTGK SLLREEVTES
     DIAEIISKWT GIPISKLVQS EMQKLLHLED ELHDRVIGQN EAVTAVADAI QRSRAGLADP
     NRPIASFIFL GPTGVGKTEL AKALAAYLFD TEDAMVRIDM SEYMEKHAVS RLIGAPPGYI
     GYDEGGQLTE AVRRRPFSVI LFDEIEKAHP DVFNVMLQIL DDGRVTDSQG RTVDFKNTII
     IMTSNIGSQY ILDVAGDDSR YEEMRSRVME AMRGSFRPEF LNRVDETIIF HSLQKDEIRN
     IIRLQVQRLA KRLDDRKMTL KLSDAALDFL ADIGYDPVYG ARPIKRAIQK EVETAIAKCI
     LRGEFSEGDT IFVDVGATER LEFKRLPSEL TVTQ
//
DBGET integrated database retrieval system