ID A0A2S9A1Z0_9MICO Unreviewed; 737 AA.
AC A0A2S9A1Z0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=ATP-dependent chaperone ClpB {ECO:0000313|EMBL:PRB07474.1};
GN ORFNames=CQ047_13940 {ECO:0000313|EMBL:PRB07474.1};
OS Microbacterium sp. MYb72.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1848693 {ECO:0000313|EMBL:PRB07474.1, ECO:0000313|Proteomes:UP000238041};
RN [1] {ECO:0000313|EMBL:PRB07474.1, ECO:0000313|Proteomes:UP000238041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb72 {ECO:0000313|EMBL:PRB07474.1,
RC ECO:0000313|Proteomes:UP000238041};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:PRB07474.1}.
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; PCOT01000025; PRB07474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9A1Z0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000238041; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 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; IPR019489; Clp_ATPase_C.
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 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; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}.
FT DOMAIN 50..194
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 452..601
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 619..710
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 264..313
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 351..378
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 737 AA; 81274 MW; 14A11A3346F5E667 CRC64;
MTTPQTEDQQ SALEQFGINL TDRARQGKLD PVIGRDNEIR RVSQVLTRRT KNNPVLIGEP
GVGKTAVVEG LAQRIVAGDV AESLKDKELV SLDISALVAG AMYRGQFEER LKSVLKEITE
SDGRVITFID ELHVLMGAGG GEGSVAASNM LKPMLARGEL RLIGATTLNE YREFIEKDAA
LERRFQQVYV GEPTVEDTIA ILRGLKGRYE AHHGVTISDS ALVAAAALSN RYLPARQLPD
KAIDLIDESM SRLKMEIDSS PVEIDQLKRQ VDRMKLEELA LKREKDAASK ERLSALREQL
VGMERQLAGL EERWARERQG LNRVGELKKQ LDDAITQRDL AMRNADYTKA SKLEYETIKR
LERDIAEAEQ AEATTSTEPR MVNEQVTDED IAAVIAAWTG IPVGRLMQGE SERLLHLESE
LGKRLIGQKD AVKAVSDAVR RSRAGISDPG RPTGSFLFLG PTGVGKTELA KALADFLFDD
EHAMVRIDMS EYGEKHSVSR LVGAPPGYVG YEQGGQLTEA VRRRPYSVIL LDEVEKAHPE
VFDVLLQVLD DGRLTDGQGR TVDFSNVILI LTSNLGSPIL IDPTLSPDDK REQVMALVRQ
AFRPEFLNRL DDIVMFSALS EDDLAQIVEL TVDALQNRLH DRRLTLAVTP DARTWLAERG
YDPVFGARPL RRLIQSEVQN RLATALLSGN VHDGDTVRVD IAADGSGLVL TAETPEPPAP
GAPASDDDVI EAELLDD
//
