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Database: UniProt
Entry: A0A0Q4VDW9_9MICO
LinkDB: A0A0Q4VDW9_9MICO
Original site: A0A0Q4VDW9_9MICO 
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
//
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