ID   A0A0X1RXU0_9BACL        Unreviewed;       987 AA.
AC   A0A0X1RXU0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:AMA63365.1};
GN   ORFNames=ASO14_843 {ECO:0000313|EMBL:AMA63365.1};
OS   Kurthia sp. 11kri321.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1750719 {ECO:0000313|EMBL:AMA63365.1, ECO:0000313|Proteomes:UP000058129};
RN   [1] {ECO:0000313|EMBL:AMA63365.1, ECO:0000313|Proteomes:UP000058129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11kri321 {ECO:0000313|EMBL:AMA63365.1,
RC   ECO:0000313|Proteomes:UP000058129};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
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DR   EMBL; CP013217; AMA63365.1; -; Genomic_DNA.
DR   RefSeq; WP_068451812.1; NZ_CP013217.1.
DR   AlphaFoldDB; A0A0X1RXU0; -.
DR   STRING; 1750719.ASO14_843; -.
DR   KEGG; kur:ASO14_843; -.
DR   PATRIC; fig|1750719.3.peg.782; -.
DR   Proteomes; UP000058129; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR   Gene3D; 3.30.980.40; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR041027; FtsK_alpha.
DR   InterPro; IPR002543; FtsK_dom.
DR   InterPro; IPR018541; Ftsk_gamma.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR22683:SF42; DNA TRANSLOCASE SFTA; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR   Pfam; PF17854; FtsK_alpha; 1.
DR   Pfam; PF09397; FtsK_gamma; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 1.
DR   SMART; SM00843; Ftsk_gamma; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50901; FTSK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000058129}.
FT   DOMAIN          653..845
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          25..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         670..677
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   987 AA;  112302 MW;  19783DC2CA3F687B CRC64;
     MKWFKNLFNK VTDEDGQEMY DRNTYEEAEE DFSYETYEEQ QREEQPKTSK GNFRFPLIDD
     VVTDSSTHSN EVNQLIEQPA VESKPLRLNR GTTPVSSKEH YSPFTAPGNS QHVAHGMSRE
     HYNPFKKSST PTTKVEIKDE PVVKPQLNKT PVPIEPAVQP KKRFVPSDVP SPVFGFKKPS
     TLTPYERKVQ ERLQAERKKN RGTLADQLVQ NRVRREERLE ASRMSVPTTP KPTEQKSESL
     TIKKHDEILV TLPKLESKVH EQPKTIQIDE VAKVTTTNEA VEIISPSEQV VEEVEVALLV
     QEKETIELAT AEVQELVTEQ VSEREEVEEL VQEQELEREE VEELVQEQEL EREEVEELVQ
     EQEPEREEVK ELVQEQVSER EEVQELVTEQ EPEREEVQEL VTEQEPEREE VQELVPAQMP
     IETPVRERSK TPINVVMLKS DKEKLQQAQA KEIVLPSWKD SKAPTNRYAV PSVKRTTEDS
     VKVEDEDSPT KVLEEELPLP STIEANVIEE VQEKIEWQVY DETLQLLREP EFQQADVEWM
     EEQGQLLVEV LAEFNVPAEI ENIVQGPTVT QFEITVGHGV KISKIKNLSD NLKLALAARD
     IRIEAPIPGK RSIGIEIPNA KARPVRLSEI VGNNSFRDSN KDLEVALGLD ITGQPVTFDL
     SEMPHGLIAG ATGSGKSVCI NSILISLLMK ASPQDVKLML IDPKIVELAV YDELPHLVSP
     VITDVKAATA ALKWAVDEME RRYQLFHHMK VRHITRYNEI VEEQRRFSLK MPYLVIVIDE
     LADLMMMAPA EVEESICRIA QKARACGIHL VLATQRPSVD VITGLIKSNI PTRIAFSVSS
     QIDSRTIIDS QGAERLLGRG DLLYLGYGKS DTVRLQGTFV TDEEIEQITE YIRSLGKPNY
     AFAPEELVQK VEQAEEQDEL FEEVCRSVAE EGSVSISSLQ RKYRIGYNRA ARLVEMMDAH
     GFVSEAKGTK PREVFLTPDQ VDSIFQQ
//