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Database: UniProt
Entry: U2Q9T2_9ACTN
LinkDB: U2Q9T2_9ACTN
Original site: U2Q9T2_9ACTN 
ID   U2Q9T2_9ACTN            Unreviewed;       522 AA.
AC   U2Q9T2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:ERK59575.1};
DE   Flags: Fragment;
GN   ORFNames=HMPREF0682_0120 {ECO:0000313|EMBL:ERK59575.1};
OS   Propionibacterium acidifaciens F0233.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=553198 {ECO:0000313|EMBL:ERK59575.1, ECO:0000313|Proteomes:UP000017052};
RN   [1] {ECO:0000313|EMBL:ERK59575.1, ECO:0000313|Proteomes:UP000017052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0233 {ECO:0000313|EMBL:ERK59575.1,
RC   ECO:0000313|Proteomes:UP000017052};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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:ERK59575.1}.
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DR   EMBL; ACVN02000112; ERK59575.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2Q9T2; -.
DR   Proteomes; UP000017052; Unassembled WGS sequence.
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   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}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}.
FT   DOMAIN          169..370
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   BINDING         187..194
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ERK59575.1"
SQ   SEQUENCE   522 AA;  56005 MW;  D77905A1B1DC67B9 CRC64;
     LPAPEPEPEP AGLAAPEHAQ MPARVEQLQL SGDVQYTLPE LSLLKPGSAP RARTAASDGL
     VDALQSVFSE FGIDAQVTGY TRGPTVTQYE VELGSGVKVE KVTALQRNIA YAVASPDVTI
     LSPIPGKSAI GIEIPNKDKE VVSLGDVLRS PQARANDKPL IVGLGKDVEG RVVLANIAKM
     PHLLVAGATG SGKSSFVNSM ITSIMVRATP DEVRMILVDP KRVELNQYEG IPHLVTPIIT
     NPKKAAQALE WVVQEMDHRY DDLAAFGFRH IDDFNKAVRA GQVQLPPGSE RELSPYPYLL
     VVVDELSDLM MVAPRDVEES IVRITQLARA AGIHLVLATQ RPSVDVVTGL IKANIPSRLA
     FATSSATDSR VILDQTGAER LVGQGDGLFL PMGAANPKRV QGSWVTEAEI REVVDRVKSQ
     LEPQYRADVT VPAGGEKKVA EDIGDDLELV LEACRQVVEL QLGSTSMLQR KLRIGFAKAG
     RIMDILETRG VVGPSEGSKP RDVLVKPDDL PETLASLSGE AA
//
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