ID A0A164D140_9SYNE Unreviewed; 871 AA.
AC A0A164D140;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB1_1 {ECO:0000313|EMBL:KZR91061.1};
GN Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=MITS9508_00299 {ECO:0000313|EMBL:KZR91061.1};
OS Synechococcus sp. MIT S9508.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR91061.1, ECO:0000313|Proteomes:UP000076799};
RN [1] {ECO:0000313|EMBL:KZR91061.1, ECO:0000313|Proteomes:UP000076799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR91061.1,
RC ECO:0000313|Proteomes:UP000076799};
RA Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT "Evolutionary Radiation of Lanthipeptides in Marine Picocyanobacteria.";
RL Submitted (FEB-2016) 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:KZR91061.1}.
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DR EMBL; LVHU01000001; KZR91061.1; -; Genomic_DNA.
DR RefSeq; WP_067092973.1; NZ_LVHU01000001.1.
DR AlphaFoldDB; A0A164D140; -.
DR STRING; 1801629.MITS9508_00299; -.
DR PATRIC; fig|1801629.3.peg.322; -.
DR Proteomes; UP000076799; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251};
KW Stress response {ECO:0000256|ARBA:ARBA00023016,
KW ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 5..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 435..527
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 96363 MW; D881197D31537ED3 CRC64;
MQPTAEQFTE KAWAAILSAQ NLAQKRRHQQ LETEHLMLAL LEQDGLASRI LEKAGVTPSA
LQSNLEAHLS QQPALQSPPE SVYLGKGLNA LLDRSESLKQ GYGDSYISIE HLLLALAEDS
RCGQRLLSQV GADAKALRTA VDAVRGSQTV TDQNPEATYE SLEKYGRDLT AAARDGKLDP
VIGRDEEIRR TIQILSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVNGDVP QALQNRQLIA
LDMGALIAGA KYRGEFEERL KAVLKEVTDS EGQIVLFIDE IHTVVGAGAT GGAMDASNLL
KPMLARGELR CIGATTLDEH RQHIEKDPAL ERRFQQVLVD QPTVEDTVSI LRGLKERYEV
HHGVRIADSA LVAAAVLSSR YIADRFLPDK AIDLVDESAA RLKMEITSKP EEIDEIDRKI
LQLEMEKLSL GRESDAASQE RLEKLERELA ELSEQQSTLN AQWQQEKGAI DELSNLKEEI
ERVQLQVDQA KRSYDLNKAA ELEYGTLATL QKQLAEKEAA LSEDNDNGQE KSLLREEVTE
DDIAEVIAKW TGIPVAKLVQ SEMAKLLGLE NQLHERVVGQ QQAVTAVADA IQRSRAGLSD
PHRPIASFLF LGPTGVGKTE LSKALAAQLF DSEDAMVRID MSEYMEKHTV SRLIGAPPGY
VGYEAGGQLT EAVRRRPYAV ILFDEVEKAH PDVFNVMLQI LDDGRVTDGQ GRTVDFTNAV
LILTSNIGSQ SILDLGGDDG QHDEMERRVN DALRGHFRPE FLNRLDDQII FHSLRRDELR
QIVSLQVNRL RQRLMERKLG LSISDNATDW LADAGYDPVY GARPLKRAIQ RELETPIAKA
ILAGRYGDGD DVTVDVQPTS GSEEQRKLVL S
//
