ID A0A158IWZ4_9BURK Unreviewed; 987 AA.
AC A0A158IWZ4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:SAL60620.1};
GN ORFNames=AWB69_06717 {ECO:0000313|EMBL:SAL60620.1};
OS Caballeronia udeis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1232866 {ECO:0000313|EMBL:SAL60620.1, ECO:0000313|Proteomes:UP000054683};
RN [1] {ECO:0000313|EMBL:SAL60620.1, ECO:0000313|Proteomes:UP000054683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 27134 {ECO:0000313|EMBL:SAL60620.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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 -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; FCOK02000063; SAL60620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158IWZ4; -.
DR Proteomes; UP000054683; 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 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; 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}; Cell cycle {ECO:0000313|EMBL:SAL60620.1};
KW Cell division {ECO:0000313|EMBL:SAL60620.1};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}.
FT DOMAIN 633..842
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 650..657
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 987 AA; 101888 MW; D2659A843BF0D95C CRC64;
MNPARGKAVP PVVSSESFFA STTSSAAVPA KPAGPPPAPE HIKETLRSIE QSTAQWTTRG
GGVDAAPEAG AVPDASGANN RQGAAALNAA GASGASGASG ASGASGALAA SANSAGSVLP
ASAPITTSVA SPASALAPSA VSASSVGVDP VNHATSSTPM PGASDLAKSA IASDSPLTPN
TNTPSPTTPS QPAASASTTQ NAIAPSPVAS TAALPDPALP TAHDNGAQQA SATNPVAAHV
DARSNPASNP ASNQPMLHVD NNRPADQTPN PTWPASIDGT APLTASGVPS NPSNGSFAHQ
EPAAPEASTS PQTAATTPTP THTSTHLADL PPWAIRAGQT HPVQTARDIA ATTPSSPVSA
SAETPSAGQV QTPPWQAEAG AARPPFRVVD TYTAPDEAEA ESEAETNVDA HSSTGTANGY
ATHAQTQTPW QTAPEAQHEP EPSPDHASNV VHFPRAGSTL TPIPAPETTP PQPDPRPPVR
GFIATEFEFH APAASAVDLP GLDLLEPASD EVEPVSEQHL AETGQLIEQR LQEFKVPVTV
VGASAGPVIT RFEVEPALGV RGSQIVGLMK DLSRGLGLTS IRVVETIPGK TCMGLELPNA
KRQMIRLSEI LEADVYRDSK SFLTIAMGKD IIGNPVVTDL ARAPHMLVAG TTGSGKSVAI
NAMILSLLFK AKPEDVRLIM IDPKMLELSV YEGIPHLLAP VVTDMKLAAN ALNWCVGEME
KRYKLMSAVG VRNLQGFNQK IRNAEAAGKK LTNPFSLTPD APEPLAKLPM IVVVIDELAD
LMMVAGKQIE QLIARLAQKA RAAGIHLILA TQRPSVDVIT GLIKANIPTR VAFQVSSKID
SRTILDQMGA ESLLGAGDML FLPPGTGYPQ RVHGAFVADE EVHSVVEYLK QFGEPEYEEG
ILSGPTPEGG TPDLFGDTPD AEADPLYDEA VSFVLRTRRA SISSVQRQLR IGYNRAARLV
EQMETAGLVS PMGTNGNREV LAPGPAD
//
