ID A0A0M2LLI5_9MICO Unreviewed; 935 AA.
AC A0A0M2LLI5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KKI18400.1};
GN ORFNames=XM48_10905 {ECO:0000313|EMBL:KKI18400.1};
OS Leucobacter sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI18400.1, ECO:0000313|Proteomes:UP000033836};
RN [1] {ECO:0000313|EMBL:KKI18400.1, ECO:0000313|Proteomes:UP000033836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI18400.1,
RC ECO:0000313|Proteomes:UP000033836};
RA Pei D., Kukutla P., Yu W., Xu J.;
RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential cell division protein that coordinates cell
CC division and chromosome segregation. The N-terminus is involved in
CC assembly of the cell-division machinery. The C-terminus functions as a
CC DNA motor that moves dsDNA in an ATP-dependent manner towards the dif
CC recombination site, which is located within the replication terminus
CC region. Required for activation of the Xer recombinase, allowing
CC activation of chromosome unlinking by recombination.
CC {ECO:0000256|ARBA:ARBA00024986}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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:KKI18400.1}.
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DR EMBL; LAYO01000102; KKI18400.1; -; Genomic_DNA.
DR RefSeq; WP_046455853.1; NZ_LAYO01000102.1.
DR AlphaFoldDB; A0A0M2LLI5; -.
DR STRING; 1642040.XM48_10905; -.
DR PATRIC; fig|1642040.3.peg.149; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000033836; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; 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: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; 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:KKI18400.1};
KW Cell division {ECO:0000313|EMBL:KKI18400.1};
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:UP000033836};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 70..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 531..731
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..902
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 548..555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 935 AA; 99206 MW; 3885F25329DF23C6 CRC64;
MASKTSTRGK AGSSSTGSRS RATAKTTVLE PVETEGVVAR AWRGLGHVVG GAARAFRIEP
IAPEDRRDGI PLLLVLLAIA GAVVEWFLIG NPVAVQLDAW SFGGLFGRVA FGLPIVMIGF
AFWLFNKPSS VHDNRRIAIG ISLAVLSIAA LCHVLGGQPQ PKNGMVALAS AGGLLGWMLG
APLSYLTLWV AVPVLSLLAA LSLLIITKTP PARIGARMGE AYRYLFGAPE KEPAADAAIE
SAPKRSRKSK ARDDDTLFDI EEEIPSGGEL PWWRRNSSGR EEDPDYSSDA QAIDEVLDGA
PSTDDRTHAF DTAFAGGETT EIPAAEANDG FPTGLFDELD QAEAAVAASG ASAASGLGDD
SPSDFVADWQ ADETPALAPT TPFAVAPPHV PAVAPSYLLP DQGTLSAGDA PRTHTDANDQ
IMAAIARVFE EFKVDARVSG FSRGPTVTQY EVELGPGVKV EKVTALSKNL SYAVASNEVR
ILSPIPGKSA IGIEIPNKDR ENVALGDVLR SAKAQRSTHP MTIGVGKDVK GGFVVANLAK
MPHLLVAGAT GSGKSSFINS MITSVLMRAT PAEVRMVLVD PKRVELTVYQ GVPHLITPII
TNPKKAAEAL QWVVKEMDMR YDDLASFGFR HIDDFNDAVR SGSIILPEGS QRVLKPYPYL
LVVVDELADL MLIAPRDVED SIQRITQLAR AAGIHLVLAT QRPSVNVVTG VIKSNVPSRY
AFAVASGTDS RVILDEVGAE RLIGQGDGLL LLNGESTPMR VQGAWVNESE IAKVVAHVKA
QAQPEYRADV AQTVEKKEID EDIGDDLEVL LAAVELVVSS QFGSTSMLQR KLRVGFAKAG
RLMDLMESRD IVGPSEGSKA RDVLVSPEQL PEVLARLRGD APPAGAVPVP PAAPPAAPQA
AEPDPYDDPI GRHQAGLEEV EADDDEDAWS LTGRD
//
