ID A0A0W7YYG3_9BURK Unreviewed; 774 AA.
AC A0A0W7YYG3; A0A1V0BBU0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KUF40141.1};
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:AQZ97321.1};
GN ORFNames=AS359_12715 {ECO:0000313|EMBL:KUF40141.1}, B5M06_02615
GN {ECO:0000313|EMBL:AQZ97321.1};
OS Comamonas kerstersii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=225992 {ECO:0000313|EMBL:KUF40141.1, ECO:0000313|Proteomes:UP000053300};
RN [1] {ECO:0000313|EMBL:KUF40141.1, ECO:0000313|Proteomes:UP000053300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12322-1 {ECO:0000313|EMBL:KUF40141.1,
RC ECO:0000313|Proteomes:UP000053300};
RA Ming D., Wang M., Hu S., Zhou Y., Jiang T.;
RT "Complete genome sequence of a multi-drug resistant strain Acidovorax sp.
RT 12322-1.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AQZ97321.1, ECO:0000313|Proteomes:UP000242792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8943 {ECO:0000313|EMBL:AQZ97321.1,
RC ECO:0000313|Proteomes:UP000242792};
RA Zheng B.;
RT "Rapid Whole Genome Sequencing of Comamonas kerstersii Causing Continuous
RT ambulatory Peritoneal Dialysis-Associated Peritonitis.";
RL Submitted (MAR-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; CP020121; AQZ97321.1; -; Genomic_DNA.
DR EMBL; LPXH01000033; KUF40141.1; -; Genomic_DNA.
DR RefSeq; WP_054067536.1; NZ_MPOF01000035.1.
DR AlphaFoldDB; A0A0W7YYG3; -.
DR STRING; 225992.B5M06_02615; -.
DR GeneID; 83038208; -.
DR KEGG; cke:B5M06_02615; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000053300; Unassembled WGS sequence.
DR Proteomes; UP000242792; 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:KUF40141.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000053300};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 421..630
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 438..445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 774 AA; 84253 MW; D0E61EE8AC1E5EA1 CRC64;
MTYSSNALNA NSSPSAPRYG LARFGHEICL IAGALGLLFW LLAMLSYSGT DPAWSTSGSG
DGGIVHNWLG RSGALLADAC YFGFGMSVWW LLLIAGYTLG SSALRWVRGQ SMEITSVRER
MKWWAGVGLL LAVSCMLEWS RLYRFEDLLP GHAGGVLGYA LGLGAVRWLG FTGSGLIGIV
LMVLALALVF RFSWGSVAEK LGAAIEAAVR LNQQKREKIK DTAEGRKAAR EREKVVEEVR
QELDDVHQHE PVLIITPTAA PAVPSERVLK ERQKPLFQDT QMQDGHLPQI DLLDAAPVKQ
ETVAPETLEM TSRLIEKKLK DFGVEVRVVQ ATPGPVVTRY EIEPATGVKG SQIVNLAKDL
ARSLSLVSIR VIETIPGKNY MALELPNAKR QSIRLSEVLG SQVYHEAKSL LTIGLGKDIE
GKPVVADLAK MPHVLVAGTT GSGKSVGINA MILSLLYKAD PKEVRLLMID PKMLEMSVYE
GIPHLLAPVV TDMKQAANGL NWCVAEMERR YKLMSKLGVR NLAGYNTKIS EAKAKGESIG
NPFSLTPEQP EPLDRLPHIV IVIDELADLM MVVGKKIEEL IARLAQKARA AGIHLILATQ
RPSVDVITGL IKANIPTRIA FQVSSKIDSR TVLDQMGAES LLGMGDMLYM ASGTGLPIRV
HGAFVSDDEV HRVVSYLKEQ GEPDYIDGVL EAATSEEGGV DGDGEVGGER DPMYDQAVEI
VLKDRKASIS YVQRKLRIGY NRSANLLEQM EKAGLVSALT ASGQREVLMP ARPE
//
