FTSK_SALTI
ID FTSK_SALTI Reviewed; 1343 AA.
AC Q8Z814;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=STY0958, t1974;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD05360.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69587.1; -; Genomic_DNA.
DR RefSeq; NP_455448.1; NC_003198.1.
DR RefSeq; WP_000076972.1; NZ_WSUP01000047.1.
DR AlphaFoldDB; Q8Z814; -.
DR SMR; Q8Z814; -.
DR STRING; 220341.16502124; -.
DR EnsemblBacteria; AAO69587; AAO69587; t1974.
DR KEGG; stt:t1974; -.
DR KEGG; sty:STY0958; -.
DR PATRIC; fig|220341.7.peg.966; -.
DR eggNOG; COG1674; Bacteria.
DR eggNOG; COG3087; Bacteria.
DR HOGENOM; CLU_001981_0_1_6; -.
DR OMA; DPFWKPG; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 Transmembrane; Transmembrane helix.
FT CHAIN 1..1343
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098288"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 25..44
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 45..74
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 75..98
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 99..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 116..132
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 133..162
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 163..179
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 180..1343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT DOMAIN 988..1201
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 357..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..823
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1008..1013
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1343 AA; 147375 MW; 2E6CD9FF44C36854 CRC64;
MSQEYTEDKD VTLTKLSSGR RLLEALLILI ALFAVWLMAA LLSFNPSDPS WSQTAWHEPI
HNLGGAPGAW LADTLFFIFG VMAYTIPVII VGGCWFAWRH QSTDDYIDYF AVSLRLIGVL
ALILTSCGLA AINADDIWYF ASGGVIGSLL STTLQPLLHS SGGTIMLLCI WAAGLTLFTG
WSWVSIAEKL GGWLLNILTF ASNRTRRDDT WVDDEEYDDE YDEETDGVQR ESRRARILRG
ALARRKRLAE KFSNPRGRQT DAALFSGKRM DDDEDIQYSA RGVAADPDDV LFSGNRATQS
EYDEYDPLLN GHSVTEPVAA AAAATAVTQT WAASADPIMQ TPPMPGAEPV VAQPTVEWQP
VPGPQTGEPV IAPAPEGYQP HPQYAQPQEA QSAPWQQPVP VASAPQYAAT PATAAEYDSL
APQETQPQWQ APDAEQHWQP EPIAAEPSHM PPPVIEQPVA TEPEPGIEET RPARPPLYYF
EEVEEKRARE REQLAAWYQP IPEPVKENVP VKPTVSVAPS IPPVEAVAAA ASLDTGIKSG
ALAAGAAAAA PAFSLATGGA PRPQVKEGIG PQLPRPNRVR VPTRRELASY GIKLPSQRIA
EEKAREAERN QYETGAQLTD EEIDAMHQDE LARQFAQSQQ HRYGETYQHD TQQAEDDDTA
AEAELARQFA ASQQQRYSGE QPAGAQPFSL DDLDFSPMKV LVDEGPHEPL FTPGVMPEST
PVQQPVAPQP QYQQPVAPQP QYQQPQQPVA SQPQYQQPQQ PVAPQPQYQQ PQQPVAPQPQ
YQQPQQPVAP QPQYQQPQQP VAPQPQYQQP QQPVAPQPQY QQPQQPTAPQ DSLIHPLLMR
NGDSRPLQRP TTPLPSLDLL TPPPSEVEPV DTFALEQMAR LVEARLADFR IKADVVNYSP
GPVITRFELN LAPGVKAARI SNLSRDLARS LSTVAVRVVE VIPGKPYVGL ELPNKKRQTV
YLREVLDNAK FRENPSPLTV VLGKDIAGDP VVADLAKMPH LLVAGTTGSG KSVGVNAMIL
SMLYKAQPED VRFIMIDPKM LELSVYEGIP HLLTEVVTDM KDAANALRWS VNEMERRYKL
MSALGVRNLA GYNEKIAEAA RMGRPIPDPY WKPGDSMDVQ HPVLEKLPYI VVLVDEFADL
MMTVGKKVEE LIARLAQKAR AAGIHLVLAT QRPSVDVITG LIKANIPTRI AFTVSSKIDS
RTILDQGGAE SLLGMGDMLY SGPNSTMPVR VHGAFVRDQE VHAVVQDWKA RGRPQYVDGI
TSDSESEGGG GGFDGGEELD ALFDQAVNFV TQKRKASISG VQRQFRIGYN RAARIIEQME
AQGIVSAQGH NGNREVLAPP PFE
