ID A0A1E3GQA1_9GAMM Unreviewed; 861 AA.
AC A0A1E3GQA1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:ODN66233.1};
GN ORFNames=A9E74_02039 {ECO:0000313|EMBL:ODN66233.1};
OS Methylophaga muralis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=291169 {ECO:0000313|EMBL:ODN66233.1, ECO:0000313|Proteomes:UP000094379};
RN [1] {ECO:0000313|EMBL:ODN66233.1, ECO:0000313|Proteomes:UP000094379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bur 1 {ECO:0000313|EMBL:ODN66233.1,
RC ECO:0000313|Proteomes:UP000094379};
RA Vasilenko O.V., Doronina N.V., Shmareva M.N., Tarlachkov S.V.,
RA Mustakhimov I., Trotsenko Y.A.;
RT "Draft Genome Sequence of Methylophaga muralis Bur 1.";
RL Submitted (JUL-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|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:ODN66233.1}.
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DR EMBL; MCRI01000024; ODN66233.1; -; Genomic_DNA.
DR RefSeq; WP_069296458.1; NZ_MCRI01000024.1.
DR AlphaFoldDB; A0A1E3GQA1; -.
DR STRING; 291169.A9E74_02039; -.
DR PATRIC; fig|291169.3.peg.2049; -.
DR Proteomes; UP000094379; 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:UP000094379};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 96031 MW; 8A9C6EEA98C425CD CRC64;
MQADKFTSKF QDALGAAQSL AVGRDHQIIE PAHLLLALLN QQGGTVKPLL AQSGVNVPAY
QADLEAQLNR FPQVEGGNGD IRISADLSRL LNQTDKLAQQ RQDQFISSEL LILAAVEDKN
QTGELLRKHG ANKTNINNVI EKIRGGERVT DQNAEEQRQA LEKYTIDLTA RAESGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GMKNKRVLAL
DMGSLIAGAK FRGEFEERLK AVLNDLSKQE GQIILFIDEI HTMVGAGKAE GAMDAGNMLK
PALARGELHC IGATTLDEYR QYVEKDAALE RRFQKVLVGE PSVESTIAIL RGLSERYEVH
HGVEITDPAI VAAANLSHRY ITDRNLPDKA IDLIDEAASR IRMEIDSKPE VLDRLERRLI
QLKIERVALQ KESDEASKKR LDTLETEMKK LAREYTDLEE VWKSEKAALH GSQHIKEELE
KARLELESAN RSGNLEKMSE LQYGRIPALE KQYDLATQAE MQEFTLLRNK VGEEEIAEVV
SKWTGIPVSK MLEGERDKLL KMDEALHQRV IGQDEAVNSV ANAIRRSRAG LSDPNRPNGS
FLFLGPTGVG KTELCKSLAT FLFDTEEAMV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
GSSIIQEMAG EDNYEAMKNA VMEIVGQHFR PEFINRVDDV VVFHPLQKSQ IRAIADIQLE
HLRQRLAEKE MGLELSDAAL DMLSEAGFDP VYGARPLKRV IQHQLENPLA QALLSGRFVA
GHVIKVDVQD EDLVFTSELR H
//