ID A0A1C6M3N2_9NEIS Unreviewed; 969 AA.
AC A0A1C6M3N2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SCK13280.1};
GN ORFNames=PSELUDRAFT_1229 {ECO:0000313|EMBL:SCK13280.1};
OS Vogesella sp. LIG4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Vogesella.
OX NCBI_TaxID=1192162 {ECO:0000313|EMBL:SCK13280.1, ECO:0000313|Proteomes:UP000198213};
RN [1] {ECO:0000313|EMBL:SCK13280.1, ECO:0000313|Proteomes:UP000198213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LIG4 {ECO:0000313|Proteomes:UP000198213};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; LT607802; SCK13280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6M3N2; -.
DR Proteomes; UP000198213; Chromosome i.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000198213}.
FT DOMAIN 613..822
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..91
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 630..637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 969 AA; 103678 MW; AB727F683AC40F5B CRC64;
MLHTLGQRVR DTLSMEEGDG VNEPAPAASD DTAPPATAKP RRNLVSEVLD ELPPAPVATP
AADTPQPEII TLPPRQPKPQ PAPPPAPELI SELPSQLPQY KHVAPPPSAE PLPVIGLAEV
QHNLQRDLKR RSPRELPQPR SGKPSRDLPL IAPEEVRASL QQLHGERYRA PDAMLGTSEP
APSSLAAYYP PDPLPHFETP LPPDERERAA SALFGPNSRF GNKEREQPAD TAASEAAPEQ
DDSTAMHDAW DGSNETAAEA ELPPATLAAS TPDSIAAAQP LPASPLPGAS ISIDTRSPWQ
LRQQGNWTAK PATPQAARFS PPAVPAPAEV PAASSPADAA QPVSEPQEIA PPAVPAPTPP
AAPLPAANPA AEAAPWDDAP RPSSWQQQPS SNGDIVWHVL DDDSAAAPDD EPAAAALRPA
SPLVWQVLDD DAAPDEGDAE DDTEDAHLGH DSSWQAAPQQ LPLMPPPRHI PVVYGDVTLP
SLELLRPAET HKAVQSEDYL IERGILIEER CAEFKVKVAV VDAYAGPVIT RYEVEPAVGV
RGSQVVNLSK DLSRALGLAS IRVVETIPGK TCMGLELPNP QRQMIRLSEI FGADVFTQSA
SKLTMALGQD ITGAPVVTDL AKAPHLLVAG TTGSGKSVGV NAMILSLLFK ATPDEVRFIM
IDPKMLELSV YNDIPHLLAP VVTDMKLAAN ALNWCVGEME KRYRLMSHLG VRNIAGYNDK
VRAAEAAGLR LTNPFTLTPE TPEPLTTLPF IVVVVDEFAD LMMVAGKKIE ELIARLAQKA
RAAGIHLILA TQRPSVDVIT GLIKANIPTR VAFQVSSKID SRTILDQMGA ESLLGQGDML
FLPPGTGYPQ RVHGAFVTDE EVHAVVEYLK QWGEPDYVEG LLTGESVADE EQLEAKGKAA
AGSEADPLYD EAVEIVLRTR KASISSVQRQ LRIGYNRAAR LIEDMEAAGI VSAMESNGNR
TVLVPQRDY
//
