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Database: UniProt
Entry: A0A0Q8P7N6_9BURK
LinkDB: A0A0Q8P7N6_9BURK
Original site: A0A0Q8P7N6_9BURK 
ID   A0A0Q8P7N6_9BURK        Unreviewed;       917 AA.
AC   A0A0Q8P7N6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=ClpV1 family T6SS ATPase {ECO:0000313|EMBL:KRB67888.1};
GN   ORFNames=ASE07_09495 {ECO:0000313|EMBL:KRB67888.1};
OS   Noviherbaspirillum sp. Root189.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB67888.1, ECO:0000313|Proteomes:UP000051303};
RN   [1] {ECO:0000313|EMBL:KRB67888.1, ECO:0000313|Proteomes:UP000051303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root189 {ECO:0000313|EMBL:KRB67888.1,
RC   ECO:0000313|Proteomes:UP000051303};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB67888.1, ECO:0000313|Proteomes:UP000051303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root189 {ECO:0000313|EMBL:KRB67888.1,
RC   ECO:0000313|Proteomes:UP000051303};
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   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {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:KRB67888.1}.
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DR   EMBL; LMHZ01000067; KRB67888.1; -; Genomic_DNA.
DR   RefSeq; WP_057293623.1; NZ_LMHZ01000067.1.
DR   AlphaFoldDB; A0A0Q8P7N6; -.
DR   STRING; 1736487.ASE07_09495; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000051303; 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; 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; IPR017729; ATPase_T6SS_ClpV1.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
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; TIGR03345; VI_ClpV1; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 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; SSF81923; Double Clp-N motif; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051303}.
FT   DOMAIN          246..391
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          638..786
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          809..902
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          168..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   917 AA;  100510 MW;  8A367E0E33537447 CRC64;
     MEIDIRTLLS KLNPECKRAM VEAAELCVKQ TQFNVELEHL LVRLIESGAP DLKLVLERFE
     VNANTVTTQL QHSMDGFKRG NGRTPALSPH FMPLFQEAWL LSSMLLGSQQ IRSGTVILAM
     LEVDSLRGLL IETAPDLLRI PRGQLRAELP TLLARSAEDA GESGHIAPGA NANANTVPNG
     TEGTLSASGP GRMPELTSGR NGHSATPSLD QFTVDMTALA REGRIDPIRG RDEEIRQIID
     ILLRRRQNNP ILTGEAGVGK TAVVEGFAQR VAQGAVPPAL ANVSVRTLDL GLLQAGAGIK
     GEFENRLKSV IAEVRASATP IILFIDEAHQ LIGAGGAEGQ GDAANLLKPA LARGELRTIA
     ATTWAEYKKY VERDPALARR FQVVKVEEPV QEVAVGMLRG MVATLEKHHG VEILDEAVLD
     AVRLSDRYIT GRQLPDKAIS VLDTACARVA IGQSGSPSQL ESLDREIMLI SEELRIMQQQ
     HARGEDRAEE ISRSEKQLKS SRERQSRLSE KLSDERCAVR EILSLRQKIA DSVNNGEEAD
     EDVRASRAAQ LQRLQKGLEA IQDDEPLVPV CVDSNIVADV ISGWTGIPVG KMLADEIHTV
     LHLKDRLGER VVGQDQALDA IARRVRTFRA ELDDPGKPVG VFMLVGPSGV GKTETAFALA
     DMLYGGERNM VTINMSEFQE AHSVSSLKGA PPGYVGYGKG GVLTEAVRRR PYSVVLLDEM
     EKAHPDVLEM FFQVFDKGTM EDGEGISIDF KNTLILLTSN AAQDVITQAC ESGRRPDVTE
     LTERLRPVLL RQFSPAFLGR VVLVPYYPLG DEQIRNIVDL KLEKLAQRFA ENHNAKFTWD
     DQVTELVTAR CTEVDSGARN IDFILTQTVL PQLSSLVLER MSMLQPFTAI HMHVSPDNQF
     AFDFQDSVLG TQFGSHA
//
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