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Database: UniProt
Entry: A0A3R8RIE3_9CORY
LinkDB: A0A3R8RIE3_9CORY
Original site: A0A3R8RIE3_9CORY 
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
//
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