ID A0A0K1F7H7_9MICO Unreviewed; 851 AA.
AC A0A0K1F7H7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ADJ73_01870 {ECO:0000313|EMBL:AKT50377.1};
OS Arsenicicoccus sp. oral taxon 190.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Arsenicicoccus.
OX NCBI_TaxID=1658671 {ECO:0000313|EMBL:AKT50377.1, ECO:0000313|Proteomes:UP000065578};
RN [1] {ECO:0000313|Proteomes:UP000065578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0371 {ECO:0000313|Proteomes:UP000065578};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (JUL-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}.
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DR EMBL; CP012070; AKT50377.1; -; Genomic_DNA.
DR RefSeq; WP_050346853.1; NZ_CP012070.1.
DR AlphaFoldDB; A0A0K1F7H7; -.
DR STRING; 1658671.ADJ73_01870; -.
DR KEGG; ars:ADJ73_01870; -.
DR PATRIC; fig|1658671.3.peg.375; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000065578; Chromosome.
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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 402..482
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 851 AA; 92032 MW; AF783D4640AEE39C CRC64;
MELTTKAAEA VNAAVHDATS AHHAQVEPAH LLVALLGQQD TTTGPLIAAT GATPQAVGAA
AARVLASLPT VTGSTSTPTA SQATQAVLQQ AGNAAAAMGD SYISTDHLLV AIARSGSFGL
DAAALEAKIP EIRGGRTITS ANPEGTFEAL EKYGTDLTQV ARDGKLDPVI GRDSEIRRVV
QVLSRRTKNN PVLIGEPGVG KTAVVEGLAQ RIVAGDVPES LRGKRLISLD LGAMVAGAKY
RGEFEERLKA VLDEIKGSDG EVITFIDEIH TIVGAGATGD SAMDAGNMLK PMLARGELRL
IGATTLDEYR ENIEKDSALE RRFQQVFVGE PSVEDTIAIL RGLKERYEAH HKVAIADSAL
VAAAALSDRY ITGRQLPDKA IDLVDEAASR LRMEIDSSPV EIDELRRQVD RLRMEELHLE
QETDAASRER LERLRKEIAD RSEELAGLNA RWEAEKAGLN KVGDLKAKLD EARSRAEVLV
REGRLNDAAP IMYGEIPRLE REVDEAQAEE QQDAGAGTAP MVQEEVDADA IADVISSWTG
IPAGRLLEGE TEKLLHMEQV IGERLIGQAE AVRAVSDAVR RARAGVADPN RPTGSFLFLG
PTGVGKTELA KSLADFLFDD ERAMVRIDMS EYSERHSVAR LVGAPPGYVG YEEGGQLTEA
VRRRPYSVVL LDEVEKAHPE TFDILLQVLD DGRLTDGQGR TVDFRNVILV MTSNLGSQFL
VDPTLDETAK REAVMATVRS SFKPEFLNRL DEVVIFDPLS MDELGHIVEL QVAEMGRRLA
DRRITLEVTE AAREWLALTG YDPAYGARPL RRLVQREIGD RLAKALLSGE VQDGQTVVVD
RDGDADALTL G
//
