ID A0A552WM93_9MICO Unreviewed; 889 AA.
AC A0A552WM93;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TRW43613.1};
GN ORFNames=FJ693_16955 {ECO:0000313|EMBL:TRW43613.1};
OS Georgenia yuyongxinii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Georgenia.
OX NCBI_TaxID=2589797 {ECO:0000313|EMBL:TRW43613.1, ECO:0000313|Proteomes:UP000318693};
RN [1] {ECO:0000313|EMBL:TRW43613.1, ECO:0000313|Proteomes:UP000318693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z446 {ECO:0000313|EMBL:TRW43613.1,
RC ECO:0000313|Proteomes:UP000318693};
RA Tian Z.;
RT "Georgenia wutianyii sp. nov. and Georgenia *** sp. nov. isolated from
RT plateau pika (Ochotona curzoniae) in the Qinghai-Tibet plateau of China.";
RL Submitted (JUL-2019) 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:TRW43613.1}.
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DR EMBL; VJXR01000073; TRW43613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A552WM93; -.
DR Proteomes; UP000318693; 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:UP000318693};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 441..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 889 AA; 95713 MW; BDA9FAA6DCE13747 CRC64;
MDTKLTTKSQ EAIAEAIRAA STAGNPQLEP VHVLAALLQQ EGGVAAALLD AVGADRGAIA
QRVRASLATL PGASGSSVAQ PQTSRATMTM ITDAGNEARA LGDEYVSTEH LLVALAASTS
PAGEVLRAAG ATREGLLAAL PTVRGTGKVT SPDPEGTFKA LEKYGQDMTA AARDGKLDPV
IGRDAEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPD SLRGKRLIAL
DLAAMVAGAK YRGEFEERLK AVLEEIKSSD GEVVTFIDEL HTVVGAGASE GSMDAGNMLK
PMLARGELRL VGATTLDEYR ERIEKDPALE RRFQQVFVGE PSVEDTVAIL RGIAPRYEAH
HKVRISDGAL VAAAALSHRY ITGRQLPDKA IDLVDEAASR LRMELDSSPI EIDELRRTVD
RLKMEELALA KSDDPASQER LEKLRADLAD RQEELASMTA RWEAEKAGHN RVGDIKAQLD
ALRTESDRAQ REGDLETASR LLYGEIPTLE RELAAAEQAE EAEAVEGAAT RQAPMVTDHV
GPDEVAEVVA TWTGIPVGRL LQGETEKLLH MEDVIGQRLI GQRTAVRAVS DAVRRSRAGV
ADPDRPTGSF LFLGPTGVGK TELAKSLADF LFDDERATVR IDMSEYSEKH SVARLVGAPP
GYVGYEEGGQ LTEAVRRRPY AVVLLDEVEK AHPEVFDILL QVLDDGRLTD GQGRTVDFRN
TILVLTSNLG SQFLVDQSLD EAAKREAVMA AVRVSFKPEF LNRLDDVVIF DALSLDELGS
IVDLQVDRLA LRLAERRLRL EVTDAAREWL ALEGYDPAYG ARPLRRLVQR EIGDKLAKML
LAGEVHDGDT LTVERADIDP AAALAQTGAL PEGQGLVLTV ATPEGAARV
//