ID A0A3R8RIE3_9CORY Unreviewed; 1175 AA.
AC A0A3R8RIE3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 08-NOV-2023, entry version 17.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:RRQ05492.1};
GN ORFNames=CXF42_01600 {ECO:0000313|EMBL:RRQ05492.1};
OS Corynebacterium bovis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=36808 {ECO:0000313|EMBL:RRQ05492.1, ECO:0000313|Proteomes:UP000278422};
RN [1] {ECO:0000313|EMBL:RRQ05492.1, ECO:0000313|Proteomes:UP000278422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-2004 {ECO:0000313|EMBL:RRQ05492.1,
RC ECO:0000313|Proteomes:UP000278422};
RA Gulvik C.A.;
RT "Twenty Corynebacterium bovis Genomes.";
RL Submitted (JAN-2018) 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:RRQ05492.1}.
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DR EMBL; PQNQ01000002; RRQ05492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8RIE3; -.
DR Proteomes; UP000278422; 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:RRQ05492.1};
KW Cell division {ECO:0000313|EMBL:RRQ05492.1};
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:UP000278422};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 193..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 752..965
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 782..789
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1175 AA; 120481 MW; F3C903867584F05C CRC64;
MSTTSRTHSQ TRPRGAGPRD AARRPTRARA PYDTTDFERT SGAFGAVGSS LGSVFGGAAR
GIGGLTRRLA TAPATRASRA DDDAVESRGQ AGGLDDDLMA EEATTVMTAS PRRGRGRGRR
RAAAGAGATG TETTGPDAPT TVVAGAGRRG AGDDGDRSDV DTAADDAATT GAGDRPGTVP
GTTRLGGGID GPAIGVVALA LVLAGTLWFG VGGAVGTGVA FALTWVVGAA ALVVPVLLAG
VAWILMVGVD VTQRSRVRLG VGTALIVLAM LGMVHIFAGQ PGDTVGRAHA GGIVGTLVGT
PMAVGFSPFL AVPLLALVVL YGGLQLTGLT VRDLARTVGD WLGFGHADDD WDGEWDDADT
SAVDAGDGDD AYGYVTGELE AAAAGDRAPR ASALRQGSRR RVGSSPMENY PVTPRDGRGA
GRGASAGAGA AAGAAGAAVN TGRADAAEPA DAADDEGRTL ELSRAARGRG RTPGRGPATR
HGAGPRSLDD NLLDDDLLDD GTADAAAPAA ASPADTPAAA GTDGATSRAD VRAAGRTAST
PVPAPREDRD TAAPAARCTR PAPTAGTVAT DGAGDTRPAD APDTGDRDPV REAARRAIAA
RSGVDAAEVT RAAAASTPAA APTPDAGPSH YDLPSTDLLV PGDAPKERSA VNDAMIDAIT
DVFEEFKVDA HVTGFSRGPT VTRYEVELGP GVKVSKITNL QSNLAYAAAT DNVRLLTPIP
GKSAVGIEVP NADREIVRLG DVLSAPEVVA DRDPMVIGLG KDIEGDFVTH SIQKMPHLLV
AGSTGSGKSA FVNSMLVSLL TRATPEEVRL ILVDPKMVEL TPYEGIPHLI TPIITQPKKA
AAALTWLVEE MEQRYMDMKS TRVRHIKDFN RKVLSGEIQT PLGSEREYRP YPYIVCVVDE
LADLMMTAPR EIEDSIVRIT QKARAAGIHL VLATQRPSVD VVTGLIKTNV PSRLAFATSS
LTDSRVILDQ PGAEKLIGMG DGLFIPQGAG RPQRIQGSFV TDEEVQAVVD AAKAQAEPDY
TEGVTEDKAA EATKDIDPDI GGDLDDLIQA VELVVTSQFG STSMLQRKLR VGFAKAGRLM
DLMETRGVVG PSEGSKAREV LVKPEELDTI LWMIKGADPA DAPKEADGGH GPAGEGDDGS
HGAGTASTPD GDAPATDGAG ASVVRATANP SRTAF
//