ID   I0KZN8_9ACTN            Unreviewed;      1465 AA.
AC   I0KZN8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Putative Cell division protein, FtsK/SpoIIIE homolog {ECO:0000313|EMBL:CCH17035.1};
GN   ORFNames=MILUP08_41954 {ECO:0000313|EMBL:CCH17035.1};
OS   Micromonospora lupini str. Lupac 08.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH17035.1, ECO:0000313|Proteomes:UP000003448};
RN   [1] {ECO:0000313|Proteomes:UP000003448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX   PubMed=22815450; DOI=10.1128/jb.00628-12;
RA   Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA   Carro L., Coll P., Trujillo M.E.;
RT   "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT   Nodules of Lupinus angustifolius.";
RL   J. Bacteriol. 194:4135-4135(2012).
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:CCH17035.1}.
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DR   EMBL; CAIE01000017; CCH17035.1; -; Genomic_DNA.
DR   RefSeq; WP_007457405.1; NZ_HF570108.1.
DR   STRING; 1150864.MILUP08_41954; -.
DR   eggNOG; COG1674; Bacteria.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000003448; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR002543; FtsK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR   PANTHER; PTHR22683:SF1; TYPE VII SECRETION SYSTEM PROTEIN ESSC; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 2.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS50901; FTSK; 2.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Cell cycle {ECO:0000313|EMBL:CCH17035.1};
KW   Cell division {ECO:0000313|EMBL:CCH17035.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000003448}.
FT   DOMAIN          1..74
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          623..815
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          959..1153
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1445..1465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          276..303
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         641..648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         976..983
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1465 AA;  155400 MW;  5D3945F4B2B16A8B CRC64;
     MRLLLTVTDQ STPATDYQVE AALDSTVAEL AEVLAQRRPE PGGRPPTLFV AGAPLDPGLT
     LADAPLWQGS VLELDRPAPV SPPRPPGPLE IRVVSGLGAG SLFPLDVGEH AIGVADDDHV
     RLNDDPLAPA LARVRVDEDG ECLLHPTGPG LLLDRVEIDD ERVWAPGAQL AAGSSLLELR
     RPVREEAALQ ISEDRTGLDY NRPPRLLPAA RTTQFTLPGP PAPPERRPLT LITVLAPVLL
     SGAAFVVTRN PLTLLFAILS PLVLIAGQIG ARRQGRATYR SRLAEYEKKK ARISGEAQEA
     LTTERLARRD NFPDPAAMAL IAVGPQRRLW ERRRTDPDFL ELRVGSADLP SEVVLRDLSQ
     DESRREVRWS ALDVPATVPV RKHGVVGVAG GAIARTTARW MMTQASALHS PEDLQIYLLC
     GADDERGWAW AGWLPHLRPR DGQDTLATVG TDTQTLARRV GELVTIISAR SGERADGAFR
     DILVVLDGAR KLRSLPGVTQ ILREGPSVGV YAICVDAEER LLPEECQAVI AQQPDGSLLV
     TQTLAAPIDD IHPDVVSPEW LSRVARALAP LRDIGGADEE SALPGASRLL DVLGMEPPEP
     DAVTARWTSG GRTTEAVLGV SLDGPFALDL KRDGPHGLVA GTTGSGKSEL LQTLVASLAV
     ANRPDAMTFV LVDYKGGSAF KDCVLLPHTV GMVTDLDTHL VSRALTSLSA ELRRREHILA
     EAGAKDIDDY VELLRREPSR VPMPRLLIVI DEFASMVRDL PDFVTGLVNI AQRGRSLGIH
     LVLATQRPGG VVSPEIRANT NLRIALRVTD SSESQDVLNA PDAASISKST PGRAFVRLAQ
     SSLVPFQAGR VGGFRPGART TARPAPWLAP LSWPDLGRPA PRRRSGEAEP SAELTDLAVL
     VGAIRDASER LAIPAQHSPW LPALPAKLSV DALPPARGSG YHLPAVAYGL VDLPAQQDQV
     PLALDLGTLG HLHIIGSSRS GRSQTLRTIG GALARVHSAA DVHLYGVDCG NGALLALGGL
     PHCGAVVQRT EAERLGRLFA RLVAELGRRQ QLLAASGSAS MVEYRAGVAA AERPPHLLLL
     LDRFEVFDKT FADYDNGTIM AGLLTLLREG AGAGIHVVLA GDRAMFSSRI SSTTDDKLVL
     RLTERGDYSM VGINHRQLPD EIEAGRAIRA SDGAEAQIAL LGDDVSGQGQ ARVLVEIAEA
     ARQRDADLGA SSRPFRIDVL PDELTLADTE ALARPAEPLW TMLGVGGDEL AALGPDLTVI
     PSLVLAGPPR SGRSTALLTM VAGLLRRGTP VVVAAPRRSP LRELAGLPGV LDLVTSENLT
     SAGLTAALEA RNGPAVVVLD DAELLLKCDA GSDLGEIARA GTEKGLGLIM AGTIDGLSGG
     FGGWHVDARR NRQGALLSPQ GLGDGELIGA KLTRGQLGVG RLGRALLHLG DGTVRLVQVP
     RTDPAALRAS VTPDRAEPQA TAAEE
//