ID A0A1W6ZF95_9BORD Unreviewed; 791 AA.
AC A0A1W6ZF95;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:ARP96073.1};
GN ORFNames=CAL15_17845 {ECO:0000313|EMBL:ARP96073.1};
OS Bordetella genomosp. 13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463040 {ECO:0000313|EMBL:ARP96073.1, ECO:0000313|Proteomes:UP000194161};
RN [1] {ECO:0000313|EMBL:ARP96073.1, ECO:0000313|Proteomes:UP000194161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU7206 {ECO:0000313|EMBL:ARP96073.1,
RC ECO:0000313|Proteomes:UP000194161};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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. Translocation stops specifically at Xer-dif sites, where FtsK
CC interacts with the Xer recombinase, allowing activation of chromosome
CC unlinking by recombination. FtsK orienting polar sequences (KOPS) guide
CC the direction of DNA translocation. FtsK can remove proteins from DNA
CC as it translocates, but translocation stops specifically at XerCD-dif
CC site, thereby preventing removal of XerC and XerD from dif.
CC {ECO:0000256|ARBA:ARBA00024784}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; CP021111; ARP96073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6ZF95; -.
DR STRING; 463040.CAL15_17845; -.
DR KEGG; bgm:CAL15_17845; -.
DR Proteomes; UP000194161; Chromosome.
DR GO; GO:0005886; C:plasma 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:0007049; P:cell cycle; 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; IPR025199; FtsK_4TM.
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; PF13491; FtsK_4TM; 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:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:ARP96073.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 431..640
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 448..455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 791 AA; 85620 MW; 764ECBC37A388590 CRC64;
MRAMPRISTA SPRASRNTRN GPSPLQTRIS ALLREARWIL FAALAAWLTL VLATWHPSDP
GWSHSVASGS IRNGGGTLGA YLGDILLYLF GYSAWWWVIL LLHRVRAGYR RLATQLRGPG
KDDPLPRVHW EEGVGFALLL VGSLGVEALR LYSWGMHLPG GTDGQSGAGG VIGQMLAGWL
SRGVGFTGGT LVLLVLVAIG LSLFFSFSWL HLAERIGSSI EGALRRVRES YTAREDRRVG
EVAQAVRTEQ VVAKQEKLVH EQPVRIEPAI TVVPRSDRAE KEKQQSLFAP PAGETDLPAL
GLLDPPQGNQ ETVSAETIEF TSRLIEKKLA DFGVSVVVVS AQAGPVITRY EIEPATGVKG
SQIVNLAKDL ARALSLVSIR VVETIPGKNL MGLELPNPRR QMVKLSEILG SQTYHASQSV
LTMALGKDIA GNPVVADLAK MPHLLVAGTT GSGKSVGINA MILSLLYKAD AAHTRLILID
PKMLEMSVYE GIPHLLAPVV TDMRQAANAL NWCVGEMEKR YRLMSKMGVR NLAGYNAKIR
DAIKREEPIP NPFSLTPDQP EPLAEMPMIV VVIDELADLM MVVGKKIEEL IARLAQKARA
AGIHLILATQ RPSVDVITGL IKANIPTRIA FQVSSKIDSR TILDQMGAET LLGQGDMLYM
PPGTGLPVRV HGAFVHDDEV HRVVESLKAQ GEPNYIEGLL EGGAEGDGGE GASSVTGIGG
DAESDPMYDQ ACEVVLKHRR ASISLVQRHL RIGYNRAARL LEQMEQSGMV SAMQSNGNRE
ILVPAREGEE A
//
