GenomeNet

Database: UniProt
Entry: A0A552WM93_9MICO
LinkDB: A0A552WM93_9MICO
Original site: A0A552WM93_9MICO 
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}.
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; 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
//
DBGET integrated database retrieval system