ID A0A2G8TCX1_9BURK Unreviewed; 785 AA.
AC A0A2G8TCX1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:PIL43882.1};
GN ORFNames=CR105_16160 {ECO:0000313|EMBL:PIL43882.1};
OS Massilia eurypsychrophila.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1485217 {ECO:0000313|EMBL:PIL43882.1, ECO:0000313|Proteomes:UP000230390};
RN [1] {ECO:0000313|EMBL:PIL43882.1, ECO:0000313|Proteomes:UP000230390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 30074 {ECO:0000313|EMBL:PIL43882.1,
RC ECO:0000313|Proteomes:UP000230390};
RA Wang H.;
RT "Massilia psychrophilum sp. nov., a novel purple-pigmented bacterium
RT isolated from Tianshan glacier, Xinjiang Municipality, China.";
RL Submitted (OCT-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}.
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:PIL43882.1}.
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DR EMBL; PDOC01000010; PIL43882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8TCX1; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000230390; Unassembled WGS sequence.
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:PIL43882.1};
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:UP000230390};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 428..637
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 445..452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 785 AA; 86176 MW; 8D87AC738474BF1E CRC64;
MTKTSQQPTN SSYTRNPTVR QPLPNRLVRL LSEARWIALA VLCLYLVIIL LSYNKGDPGW
SHDVVVNKVS NLGGRAGAWL ADLMLFIFGF SAWWWVVCVL RLVWKDYRAL TQKFVMEAQF
DPEHQHEAVI RWTGFVLLVI GSLGLEYLRM YSLQVQLPRA PGGVLGQLIG QGALSFGFTG
ATLLLLLLFG IGLSLFFHIS WLAVAERIGE YIEMTIDWFR LRYQDREDRK QGEVAAVKRD
EVVVIERAKH VEKHIDSPPV KIEPHAAPVI VKSERVEKEK QAPLFRDLPG DSPLPPLSLL
DEAAEYQETV SVETLEFTSR LIEKKLSDFG VDAKVVAAFP GPVVTRYEIE PATGVKGSQI
VGLARDLARS LSLTSLRVVE TIPGKNYMAL ELPNPKRQIV RLTEIVGSKI YNDSPSSLTI
ALGKDIAGKP VIADLAKMPH LLVAGTTGSG KSVGINATIL SLLYKSDPAD VRLILIDPKM
LEMSVYEGIP HLLAPVVTDM RQAGHALNWA VNEMERRYKL MSKLGVRNLA GYNAKIADAA
KREEHIPNPF SLTPDSPEPL EKLPTIVIII DELADLMMVV GKKVEELIAR IAQKARAAGL
HLILATQRPS VDVITGLIKA NIPTRIAFQV SSKIDSRTIL DQMGAEALLG MGDMLYMPPG
TGLPVRVHGA FVSDEEVHRV VKHLLQTGEP NYIDGILEGG TLEGEGGADG APAGEGGGEA
DALYDQAVQV VLKNRRASIS LVQRHLRIGY NRAARLLEQM ENSGVVSSMQ SNGNREILVP
AASAE
//
