ID A0A0Q4VDW9_9MICO Unreviewed; 890 AA.
AC A0A0Q4VDW9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=AAA family ATPase {ECO:0000313|EMBL:KQO64861.1};
GN ORFNames=ASF23_01375 {ECO:0000313|EMBL:KQO64861.1};
OS Curtobacterium sp. Leaf261.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO64861.1, ECO:0000313|Proteomes:UP000050821};
RN [1] {ECO:0000313|EMBL:KQO64861.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO64861.1,
RC ECO:0000313|Proteomes:UP000050821};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO64861.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO64861.1,
RC ECO:0000313|Proteomes:UP000050821};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
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:KQO64861.1}.
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DR EMBL; LMMJ01000001; KQO64861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4VDW9; -.
DR STRING; 1736311.ASF23_01375; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000050821; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; 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 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000050821};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 44..188
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 181..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 95099 MW; 93870935BFE3C51B CRC64;
MPDNTDQSNT GEPSSFDAFL ARLLANAGAA EEQRRVPFGR PVDIARLLSR RTHEVLRATA
EYAVGRGDHE LDALHLLRVL VTSDPFAAVV RAAGVDPDAF AETIEDRLPE SSSGARPVAR
PALTPSAQRV LLDATQSARA FGSTYVDPEH VFFALVVEQD TVAGQLLAAA GVTPETMQAY
AQDAARAAQE GRPAPGTELD TASESDTPTL DRFGTDLTAL AREGGIDPVI GRTAEIEQTV
EILLRRTKNN PVLIGEPGVG KTAIVAGLAQ RIADGDVPAL LRGRRVVSLD LAAMLSGTKY
RGDFEERLTN AMDEIAAHRD ELIVFVDELH TVVGAGGGGD GGSMDAGNIL KPRLARGDLH
LVGATTLSEY RRIEKDAALE RRFQPVQVAE PSVSDAVQIL AGLAPRYEEH HGVTYSEGAI
RAAVEMSHRY VADRFLPDKA IDLIDQAGAR RRLALSGSED VDALRAEVVG LQVEKDAAVA
AERYEDASGI RDRIDGLEAR IASATSPSVA VVAGSASSGV TDRTDASRAS RQSGAGPTTA
AEPDVVITEA DIAEMVSRST GIPAARLSAD DRTRLAALES ELHGRVVGQD DAVTAIAKAV
RRSRSGMGDP RRPVGSFLFL GPTGVGKTEL AKTLASSLFG DESAMLRFDM SEFGERHTVS
RLVGAPPGYV GYDEAGQLTE RVRRNPYSVI LLDEIEKAHP DVFNLLLQVL DDGHLTDGQG
RTVDFRNTVV IMTSNLGSEF LASRSGALGF SAAADGGFTE SDLRNRVMGR LRESMRPEFL
NRIDEIVLFR KLDRAQLRTI VGLLLDDTRL RLAAQDVALT ISDGAVDWIV DHGYEPEYGA
RPLRRVVQRE VEDRIADLVV ASATSAGDVV EISVADDALV ATVSHPALLV
//