FTSK_PASMU
ID FTSK_PASMU Reviewed; 930 AA.
AC Q9CP13;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=PM0255;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
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DR EMBL; AE004439; AAK02339.1; -; Genomic_DNA.
DR RefSeq; WP_010906546.1; NC_002663.1.
DR AlphaFoldDB; Q9CP13; -.
DR SMR; Q9CP13; -.
DR STRING; 747.DR93_1805; -.
DR EnsemblBacteria; AAK02339; AAK02339; PM0255.
DR KEGG; pmu:PM0255; -.
DR PATRIC; fig|272843.6.peg.263; -.
DR HOGENOM; CLU_001981_7_1_6; -.
DR OMA; DMLYSGA; -.
DR Proteomes; UP000000809; 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; 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 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; 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 Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..930
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098277"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 573..786
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 593..598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 930 AA; 103039 MW; E0BE111D5762053F CRC64;
MIKRISEKFT PKQYLLAFFF LVGMLFGVYL IVAWSSYSPL DNSWASSSYI PTTINKAGRF
GAWFIDLFFV LFGHVGHIIP FLIFGISFYF WRRKGKVPFS FFRLSLWLLG FSIFLCGVCV
LFTLLFSNTP YYLSGGVLGG SLVTAFFPML DFVGLMLSGT LLALLGFVLC SGTSLIRSCI
YFYDWLTMKN PTQTQEEETI STTPVQQELA LQEEPSIQSI NEGERVFVSE APSATMDEEK
SLINIENLIQ IQGLESASQA KESTIPTVPL DDVNQVELGG YAVEPELALP SVSVAFVEDT
ALSSSEAEHE DSKPFTTQIP HTAGEPLVAT EFAMPKVSLS PLDTSLSDNS EIAREDESDL
ARQFAAQEQQ RREEMALRAK ALNAEEALQT ILAEPEIRQN STADVSDSTT PHYKPYGESL
IHPALQQKVT TQVKPTTPMP SLDLLEHRPS QAHRITQEEI IETSQRIEHQ LRNFGVKATV
KDVLVGPVVT RYELELQPGV KASKVSSIDT DLARALMFRS IRVAEVIPGK PYIGIETPNV
NRQMVTLREV LDSDVFRQSN SLLSMALGKD ISGKPVVVDL AKMPHLLVAG STGSGKSVGV
NTMILSLLFR VKPEEVKFIM IDPKVVELSI YDGIPHLLTE VVTDMKKAAN ALRWCVDEME
RRYQLLSALR VRNIEGYNEK IEEYEAMNMP IPNPIWRPGD TMDTLPPALE KLSYIVVIVD
EFADLMMVAG KQVEELIARL AQKARAIGIH LILATQRPSV DVITGLIKAN IPSRIAFTVA
SKIDSRTILD QVGAEALLGR GDMLYSGAGS SDLVRVHGAF MSDDEVARVV DDWKARGKPN
YIEGILDSGE DEATESNGAN SDAGELDDLF DEVVEFVTST GTTSTSYIQR KFRVGFNRAA
RIMDQLEEQG IVSAMQNGKR EVLARRSSDF
