FTSK_CAMJJ
ID FTSK_CAMJJ Reviewed; 946 AA.
AC A1VZM0; Q46089; Q9PP45;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; Synonyms=ftsQ; OrderedLocusNames=CJJ81176_0893;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8063102; DOI=10.1016/0378-1119(94)90830-3;
RA Miller S., Pesci E.C., Pickett C.L.;
RT "Genetic organization of the region upstream from the Campylobacter jejuni
RT flagellar gene flhA.";
RL Gene 146:31-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) 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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Located at the septum.
CC {ECO:0000250}.
CC -!- DOMAIN: Consists of an N-terminal domain, which is sufficient for the
CC localization to the septal ring and is required for cell division,
CC followed by a linker domain, and a C-terminal domain, which forms the
CC translocation motor involved in chromosome segregation. The C-terminal
CC domain can be further subdivided into alpha, beta and gamma subdomains.
CC The alpha and beta subdomains multimerise to produce a hexameric ring,
CC contain the nucleotide binding motif and form the DNA pump. The gamma
CC subdomain is a regulatory subdomain that controls translocation of DNA
CC by recognition of KOPS motifs and interacts with XerD recombinase (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61512.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U06951; AAA61512.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000538; EAQ72446.1; -; Genomic_DNA.
DR RefSeq; WP_011812744.1; NC_008787.1.
DR AlphaFoldDB; A1VZM0; -.
DR SMR; A1VZM0; -.
DR STRING; 354242.CJJ81176_0893; -.
DR PRIDE; A1VZM0; -.
DR EnsemblBacteria; EAQ72446; EAQ72446; CJJ81176_0893.
DR KEGG; cjj:CJJ81176_0893; -.
DR eggNOG; COG1196; Bacteria.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_8_1_7; -.
DR OMA; VHEHSQQ; -.
DR Proteomes; UP000000646; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF17854; FtsK_alpha; 1.
DR Pfam; PF09397; FtsK_gamma; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..946
FT /note="DNA translocase FtsK"
FT /id="PRO_0000281902"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..946
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 620..810
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 640..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT CONFLICT 103
FT /note="S -> Y (in Ref. 1; AAA61512)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..144
FT /note="EN -> VF (in Ref. 1; AAA61512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 946 AA; 108070 MW; DA64002A3842DC8E CRC64;
MLAPGMGEWV YKANLFLFGE FGYYYPFSLL ILNYLYYKKK YKIENFKRRE LFGFSLAFFS
TLLLFSVFYR EFGYILEIVY GFFSIILGRT GSGIFALLLL LFSLVLLFPK FAKEILKIEL
DFTYLLKVEQ AFKSLLMRVF GGENEKEDVG KSEPIAPKLN ILQDSIYGNL QINKKGETNN
LEQIIKDSNI NASKNSITTA KENFEKLKNQ ILDETIEIDK QSLKESRSFV HEHSQQVRNF
AQKASKMSIS LDEDFNFISE EEVDMIPERF LKPKKLEDIK QIDTNKNLDE PSYKRKNIEI
PVSNQEVKPK IFTKELELRE NLIKKEKLEQ EYKAYQNEIL ENKVKQEIKK LEEYDAINSS
DIIEGNKYSF NSPKTIKAET EESDKINENK NLDKADNIFE FAPIVEELNH PYIEPTPIKN
INEIVIEEKN TLDFIQNTET KIDNEKTNDQ EIKLQKAVLA KEIAINQALL REIEQGEVEK
PKDFTLPPLD FLANPKEHKQ EINESEIDKK IYNLLEKLRR FKIGGDVIST YVGPVVTTFE
FRPSADVKVS RILNLQDDLT MALMAKSIRI QAPIPGKDVV GIEVPNDEIQ TIYLREILQS
EVFKNAKSPL TIALGKDIVG NAFVTDLKKL PHLLIAGTTG SGKSVGINSM LLSLLYRNSP
KTLRLMMIDP KMLEFSIYND IPHLLTPVIT DPKKAVNALS NMVAEMERRY RLMADAKTKN
IENYNEKMKE LGGEELPFIV VIIDELADLM MTAGKDVEFY IGRLAQMARA SGIHLIVATQ
RPSVDVVTGL IKANLPSRIS YKVGQKIDSK VILDAMGAES LLGRGDCLFT PPGTSSIVRL
HAPFASEFEI EKIVDFLKDQ QSVEYDESFL KDQQSVGVTT NESFDGEVDE LYEEAKRVIL
EDGKTSISYL QRRLKIGYNR SANIIEQLTQ NGILSEPDAK GQREIL
