ID A0A368N1S2_9FLAO Unreviewed; 863 AA.
AC A0A368N1S2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RCU44120.1};
GN ORFNames=DQ356_03660 {ECO:0000313|EMBL:RCU44120.1};
OS Chryseobacterium lacus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2058346 {ECO:0000313|EMBL:RCU44120.1, ECO:0000313|Proteomes:UP000252172};
RN [1] {ECO:0000313|EMBL:RCU44120.1, ECO:0000313|Proteomes:UP000252172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLOS41 {ECO:0000313|EMBL:RCU44120.1,
RC ECO:0000313|Proteomes:UP000252172};
RA Li C.-M.;
RT "Chryseobacterium lacus sp. nov., isolated from lake water.";
RL Submitted (JUL-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:RCU44120.1}.
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DR EMBL; QPIE01000002; RCU44120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368N1S2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000252172; 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:UP000252172};
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..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 97880 MW; 8272E25A9A4DBF24 CRC64;
MNLNQFTVKS QEAIQKAQQI AMEFGNQSIE PQHLLEGIFQ IDDSVSEFLL KKSEAEVTLV
RERNRALIEK LPKVEGGNLY LSQTANKILL DAPNIAKKMG DEYVTIEHFW LSLFEVNSEV
SKILKDMGIT KNSLEAAIKE LRKGSRATSA SSEETYQSLN KYAKNFNELA AEGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP ILIGEPGVGK TAIAEGIAHR IISGDVPENL MDKTLYSLDM
GALIAGAKYK GEFEERLKSV VNEVIKSDGQ IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAVG ATTLNEYQKY FEKDKALERR FQKVMVEEPD TESAISILRG IKDKYEAHHK
VRIKDEAIIA AVEQSQRYIS DRFLPDKAID LIDEASAKLR MEINSKPEEL DVLDRKLMQL
EIELAAISRE GNQVQINHIK EDIAKVSEER NEINAKWLKE KQKSEDLTQI KKEIESLKLE
AERASRAGDY AKVAEIQYGK LRNKEEELKK MELEMQNSQN ELIKEEVTAE HISEVISKWT
GIPVTKLLKS EREKLLHLED ELHKRVVGQE EAIEAVADAI RRNRAGLNDE KKPIGSFLFL
GTTGVGKTEL AKALAEFLFD DENNMTRIDM SEYQERHSVS RLVGAPPGYI GYEEGGQLTE
AVRRRPYSVV LLDEIEKAHP DVFNTLLQVL DDGRLTDNKG RVVNFKNSII IMTSNMGSQL
IQENFENLTD DNRYEVIEKT REEVFTLLKQ TLRPEFLNRI DEVVLFQPLT RKEIGKIVQY
QLRGFNKMLE KKGILMTTTE DAIEYIMNKG YDPSFGARPL KRVLQQEVLN KLSKEILAGN
VNDGDRITLD YFEESGLVFR QTE
//
