ID A0A0M2PS32_PROHO Unreviewed; 877 AA.
AC A0A0M2PS32;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=PROH_16600 {ECO:0000313|EMBL:KKI99325.1};
OS Prochlorothrix hollandica PCC 9006 = CALU 1027.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Prochlorotrichales;
OC Prochlorotrichaceae; Prochlorothrix.
OX NCBI_TaxID=317619 {ECO:0000313|EMBL:KKI99325.1, ECO:0000313|Proteomes:UP000034681};
RN [1] {ECO:0000313|EMBL:KKI99325.1, ECO:0000313|Proteomes:UP000034681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CALU 1027 {ECO:0000313|EMBL:KKI99325.1};
RA Shanker A., Yadav P., Khan S., Sharma V.;
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKI99325.1, ECO:0000313|Proteomes:UP000034681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CALU 1027 {ECO:0000313|EMBL:KKI99325.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) 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:KKI99325.1}.
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DR EMBL; AJTX02000006; KKI99325.1; -; Genomic_DNA.
DR RefSeq; WP_017712865.1; NZ_KB235937.1.
DR AlphaFoldDB; A0A0M2PS32; -.
DR STRING; 317619.GCA_000332315_02506; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000034681; 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:UP000034681};
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..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 877 AA; 98646 MW; E2DC0B00F280CAB7 CRC64;
MQPTDANQFT EKAWAAIAKA PDVAKQARHQ QLESEHLFKA LLEPQGLAAS IIAKRGVRLD
RLQDYTQQFI DRQPKVSGNS DSIYLGQSLD QLLDRADRHR QDLKDDYISI EHLLLAYSKD
KRFGQKLFQE FNWTESDFKK TIKEIRGSQT VTDQNPEGKY QSLEKYGRDL TEFARLGKLD
PVIGRDDEIR RTIQILSRRT KNNPVLIGEP GVGKTAIAEG LAQRIVNGDV PESLKDRKLI
TLDMGSLIAG AKYRGEFEER LKAVLKEVTE SEGQIILFID EIHIVVGAGS GQGSMDASNL
LKPMLARGEL RCIGATTLDE YRQYIEKDAA LERRFQQVYI DQPSVEDTIS ILRGLKDRYE
THHNVKIADG ALVAAAILST RYISDRFLPD KAIDLVDEAA ARLKMEITSK PEELDEVDRK
ILQLKMEKSS LQKETDLASL DRLSRLEKEL ADLQEIQSGL NAQWQSEKDT LDRRKTIKDK
IEAVNLDLQQ AKRDYDYNRA AELEHGTLPQ LQRQLLEADE QFAHAQTSGK SLLREEVTEE
DIAEIISKWT GIPISKLVES EMQKLLQLED ELHQRVVGQR DAVTAVADAI QRSRAGLSDP
NRPTASFIFL GPTGVGKTEL AKALAAYLFD TEEAIVRIDM SEYMEKHAVA RLIGAPPGYV
GYEEGGQLTE AVRRRPYAVV LFDEIEKAHP DVFNIMLQIL DDGRITDSQG HTVDFKNTII
IMTSNIGSSL ILDVVGDDSR YEEMRGRVME SLRENFRPEF LNRIDETIIF HGLDQSELRQ
IVQIQIQGLG ARLADRKLGL SLSEAALDFL AAVGYDPVYG ARPLKRAIQR ELETPIAKGI
LRGEFQSGAV IVVEEENERL CIRSQTPAPP TESGNPA
//