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Database: UniProt
Entry: A0A0U4FA79_9BACI
LinkDB: A0A0U4FA79_9BACI
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ID   A0A0U4FA79_9BACI        Unreviewed;       763 AA.
AC   A0A0U4FA79;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:ALX50518.1};
GN   ORFNames=AOX59_02615 {ECO:0000313|EMBL:ALX50518.1};
OS   Lentibacillus amyloliquefaciens.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX   NCBI_TaxID=1472767 {ECO:0000313|EMBL:ALX50518.1, ECO:0000313|Proteomes:UP000050331};
RN   [1] {ECO:0000313|EMBL:ALX50518.1, ECO:0000313|Proteomes:UP000050331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LAM0015 {ECO:0000313|EMBL:ALX50518.1,
RC   ECO:0000313|Proteomes:UP000050331};
RA   Wang J.-L., He M.-X.;
RT   "Complete genome sequence of strain Lentibacillus amyloliquefaciens
RT   LAM0015T isolated from saline sediment.";
RL   Submitted (JAN-2016) 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; CP013862; ALX50518.1; -; Genomic_DNA.
DR   RefSeq; WP_068448099.1; NZ_CP013862.1.
DR   AlphaFoldDB; A0A0U4FA79; -.
DR   STRING; 1472767.AOX59_02615; -.
DR   KEGG; lao:AOX59_02615; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000050331; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; 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; IPR003593; AAA+_ATPase.
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:SF41; DNA TRANSLOCASE FTSK; 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; SM00382; AAA; 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}; Cell cycle {ECO:0000313|EMBL:ALX50518.1};
KW   Cell division {ECO:0000313|EMBL:ALX50518.1};
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000050331};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        50..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          424..623
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          207..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         441..448
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   763 AA;  84340 MW;  5D2163FA38A1AFC7 CRC64;
     MAKKKRRKKK SQLNKQVKYE LLGLLFIFLA IFGSGASAIS DGAIPGGLEY IFRFFLGIWY
     FIASIFLLVT GIVLMVKRRY PDFSHKKLIG FYIIFTGVLL LTHIQTYERL LVSSEETSIL
     AATWDQFFAY VDGAGGGFQT GGGMIGGLLF TFCYYLFSSV GAKIVSVFSI LIGIIFMTEF
     SLGQFFSKSS KRFGNLFTSI KERLRSSRAG HLPNQEDNTR DAPDPQQETG GYDEPVIQDF
     TDVAYSFSTH DTGTDETHSE ANTDNPEATE TKEGQGDPLP MTEAENHEYE LPSPNLLTEP
     TQNSQQQEKS QIQATVRKLE RTFDSFGVKA KVTKVHVGPA VTKYEVYPEA GVKVSKIVNL
     HDDLALALAA KDIRIEAPIP GKSAVGIEVP NQEIAQVSLR EVLDTSTSNQ SSKLLFALGR
     DISGESIVSE LSKMPHMLIA GATGSGKSVC VNGIITTILM RAKPHEVKMM MIDPKKVELN
     VYNGIPHLLT PVVTDPKKAS RALKKVVSEM ERRYELFSET GTRNIEGYNE YIRKYNQTVA
     SEEEKQPNLP YIVVLVDELA DLMMVASNDV EDAITRLAQM ARAAGIHLIL ATQRPSVDVI
     TGVIKANIPS RIAFSVSSAT DSRTILDAGG AEKLLGRGDM LFMPVGSSKP TRVQGAFLSD
     EEVERIVDHC IEQQKASYQE EMIPEETSEA VSDVDDELYD DAVQMITEMQ SASVSMLQRR
     FRIGYTRAAR LIDAMEDHGI VGPYEGSKPR QVLVSQPSEE RTS
//
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