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Database: UniProt
Entry: L0DDI1_SINAD
LinkDB: L0DDI1_SINAD
Original site: L0DDI1_SINAD 
ID   L0DDI1_SINAD            Unreviewed;       888 AA.
AC   L0DDI1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Type VI secretion ATPase, ClpV1 family {ECO:0000313|EMBL:AGA26731.1};
GN   OrderedLocusNames=Sinac_2420 {ECO:0000313|EMBL:AGA26731.1};
OS   Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS   MOB10).
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Singulisphaera.
OX   NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA26731.1, ECO:0000313|Proteomes:UP000010798};
RN   [1] {ECO:0000313|EMBL:AGA26731.1, ECO:0000313|Proteomes:UP000010798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC   {ECO:0000313|Proteomes:UP000010798};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003364; AGA26731.1; -; Genomic_DNA.
DR   RefSeq; WP_015245883.1; NZ_JH621478.1.
DR   AlphaFoldDB; L0DDI1; -.
DR   STRING; 886293.Sinac_2420; -.
DR   KEGG; saci:Sinac_2420; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_1_2_0; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000010798; Chromosome.
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; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
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; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
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; PF02861; Clp_N; 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; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          8..155
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          155..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          434..485
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   888 AA;  97077 MW;  74A9279340D4DEBA CRC64;
     MGVDSGAVIK TLNKTCVNSL QAAAGLCLSR TNYSVEVEHW LLKLTEVHDS DLARVFRHFE
     VNTSHLQRDL TKALDRLKTG NARTPMLSPS IDELIRSAWV LASLQYQSRQ VRSGFLLLAL
     LEDEQLGRLA RDASPEFAKI KVETLASGMT SLIAGSAEEE SPAREAEGQA TPSRGAATQT
     PALDQYTINL TERARAGQID PVLGRDAEVR QMVDILIRRR QNNPILTGEA GVGKTAVVEG
     LAARIAAGDV PEPLRKVVLR TLDLGLLQAG AGVKGEFENR LKQVIAEVKA SPVPIVLFID
     EAHTMIGAGG QAGQGDAANL LKPALARGEL RTIAATTWAE YKKYFEKDAA LARRFQVIRV
     EEPSEEKAIV MMRGITAMLE SHHGVRILDE AVEGSVKLSA RYIPGRQLPD KSVSLLDTAC
     ARVAISQTAI PPAVEDCRRR IDHLKVEIGI LERENVTGVQ HDARLAETRE ALAKSESLLV
     ELEKRWKEER TLVQTIRGLA EQIEKAHAAK NGKAGELPTI ETPAQPDKLK TELATRTLEL
     SALQGDSPLM HVNVDSQTIA AVIAGWTGIP VGKMLADEIR TVLNLKTKLE ERVIGQAQAL
     EAVSQRIRTA RANLTDPRRP IGVFLLVGPS GVGKTETAIS LADSLYGGER NLVVINMSEY
     QEAHTVSGLK GSPPGYVGYG EGGVLTEAVR RKPYCVVLLD EVEKAHPDVM ELFFQVFDKG
     TLEDGEGRVI DFKNTVILLT SNVGTETTMA LCADEDTTPE AAGLVEALRP ELLKVFPPAL
     LGRLVVVPYY PISDEVMKQI VRLQLDRIVR RVRENHKAAF TYSEEIVANI ASRCKEVHSG
     ARNVDQILTR SLLPELSQEF LARMAEGDVL TSVYVDVDEQ GNFRYQFS
//
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