ID   D8FZU8_9CYAN            Unreviewed;       611 AA.
AC   D8FZU8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Vesicle-fusing ATPase {ECO:0000313|EMBL:CBN55888.1};
DE            EC=3.6.4.6 {ECO:0000313|EMBL:CBN55888.1};
GN   ORFNames=OSCI_2530011 {ECO:0000313|EMBL:CBN55888.1};
OS   Kamptonema sp. PCC 6506.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Kamptonema.
OX   NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN55888.1, ECO:0000313|Proteomes:UP000004532};
RN   [1] {ECO:0000313|Proteomes:UP000004532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX   PubMed=20675499; DOI=10.1128/JB.00704-10;
RA   Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT   "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT   reveals several gene clusters responsible for the biosynthesis of toxins
RT   and secondary metabolites.";
RL   J. Bacteriol. 192:5264-5265(2010).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
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; CACA01000221; CBN55888.1; -; Genomic_DNA.
DR   RefSeq; WP_007355103.1; NZ_CACA01000221.1.
DR   AlphaFoldDB; D8FZU8; -.
DR   OrthoDB; 548807at2; -.
DR   Proteomes; UP000004532; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd19503; RecA-like_CDC48_NLV2_r1-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR   PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Hydrolase {ECO:0000313|EMBL:CBN55888.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004532}.
FT   DOMAIN          121..257
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          387..525
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          33..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  66585 MW;  9B93FFD6FB7F316D CRC64;
     MNDLFKGFDQ LLELAKTLEE KIQSGELKAD VQVNTRPLSS VPRQGNIPRS GTPKTDIGTT
     RIRTQPTSTE TTGPEPSVTP PTQIPSLQDV GGLGQVLKEL KELVAIPLKR PELLEKLGLE
     PTKGVLLVGP PGTGKTLTAR ALADELGVNY IALAGPEVMS KYYGEAEQKL RAIFEKAAKN
     APCLVFIDEI DSLAPDRSKV EGEVEKRLVA QLLSLMDGFA QTKGVILLAA TNRPDHLDPA
     LRRPGRFDRE VHFPVPDCQG RLEILQILTR SQPLDETVNL SAIADLAVGF VGADLKAVCQ
     KAAYSALRRH IPELEAVIPD TMSVTHSDFL QALKEIKPAV LRSVEIESPN VPWEEIGGLE
     SIKQTLRESV EGALLHPELY RQTKAIAPRG ILLWGPPGTG KTLLAKAVAS QARANFICVN
     GPELLSRWVG ASEQAVRELF TKARQASPCV VFIDEIDSLA PARGRHSGDS GVSDRVVGQL
     LTELDGLHNS ANVLLIGATN RPEIIDPALL RSGRLDLQLK VDLPNLENRL AILEIHNQDR
     PLERVDLGYW ATLTEGWNGA DLALFSNQAA VEAIRCYRAQ SLPDASAIQI TTTHFSTAYE
     RLAEQRQSVN R
//