FTSK_SHIFL
ID FTSK_SHIFL Reviewed; 1342 AA.
AC Q83S00;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=SF0849, S0890;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN42482.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16354.1; -; Genomic_DNA.
DR RefSeq; NP_706775.1; NC_004337.2.
DR RefSeq; WP_000077083.1; NZ_WPGW01000037.1.
DR AlphaFoldDB; Q83S00; -.
DR SMR; Q83S00; -.
DR STRING; 198214.SF0849; -.
DR EnsemblBacteria; AAN42482; AAN42482; SF0849.
DR EnsemblBacteria; AAP16354; AAP16354; S0890.
DR GeneID; 1023821; -.
DR KEGG; sfl:SF0849; -.
DR KEGG; sft:NCTC1_00850; -.
DR KEGG; sfx:S0890; -.
DR PATRIC; fig|198214.7.peg.979; -.
DR HOGENOM; CLU_001981_0_1_6; -.
DR OrthoDB; 349533at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..1342
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098291"
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..1342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT DOMAIN 987..1200
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 346..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..822
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1007..1012
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT CONFLICT 446
FT /note="Q -> L (in Ref. 2; AAP16354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1342 AA; 148192 MW; 08F69F638C973C44 CRC64;
MSQEYTEDKE VTLTKLSSGR RLLEALLILI VLFAVWLMAA LLSFNPSDPS WSQTAWHEPI
HNLGGMPGAW LADTLFFIFG VMAYTIPVII VGGCWFAWRH QSSDEYIDYF AVSLRIIGVL
ALILTSCGLA AINADDIWYF ASGGVIGSLL STTLQPLLHS SGGTIALLCV WAAGLTLFTG
WSWVTIAEKL GGWILNILTF ASNRTRRDDT WVDEDEYEDD EEYEDENHGK QHESRRARIL
RGALARRKRL AEKFINPMGR QTDAALFSGK RMDDDEEITY TARGVAADPD DVLFSGNRAT
QPEYDEYDPL LNSAPITEPV AVAAAATTAT QSWAAPVEPV TQTPPVASVD VPPSQPTVAW
QPVPGPQTGE PVIAPAPEGY PQQSQYAQPA VQYNEPLQQP VQPQQPYYAP AAEQPAQQPY
YAPAPEQPVA GNAWQAEEQQ STFAPQSTYQ TEQTYQQPAA QEPLYQQPQP VEQQPVVEPE
PVVEETKPAR PPLYYFEEVE EKRAREREQL AAWYQPIPEP VKEPEPIKSS LKAPSVAAVP
PVEAAAAVSP LASGVKKATL ATGAAATVAA PVFSLANSGG PRPQVKEGIG PQLPRPKRIR
VPTRRELASY GIKLPSQRAA EEKAREAQRN QYDSGDQYND DEIDAMQQDE LARQFAQTQQ
QRYGEQYQHD VPVNAEDADA AAEAELARQF AQTQQQRYSG EQPAGANPFS LDDFEFSPMK
ALLDDGPHEP LFTPIVEPVQ QPQQPVAPQQ QYQQPQQPVA PQQQYQQPQQ QVAPQPQYQQ
PQQPVAPQQQ YQQPQQPVAP QPQYQQPQQP VAPQPQYQQP QQPVAPQPQD TLLHPLLMRN
GDSRPLHKPT TPLPSLDLLT PPPSEVEPVD TFALEQMARL VEARLADFRI KADVVNYSPG
PVITRFELNL APGVKAARIS NLSRDLARSL STVAVRVVEV IPGKPYVGLE LPNKKRQTVY
LREVLDNAKF RDNPSPLTVV LGKDIAGEPV VADLAKMPHL LVAGTTGSGK SVGVNAMILS
MLYKAQPEDV RFIMIDPKML ELSVYEGIPH LLTEVVTDMK DAANALRWCV NEMERRYKLM
SALGVRNLAG YNEKIAEADR MMRPIPDPYW KPGDSMDAQH PVLKKEPYIV VLVDEFADLM
MTVGKKVEEL IARLAQKARA AGIHLVLATQ RPSVDVITGL IKANIPTRIA FTVSSKIDSR
TILDQAGAES LLGMGDMLYS GPNSTLPVRV HGAFVRDQEV HAVVQDWKAR GRPQYVDGIT
SDSESEGGAG GFDGAEELDP LFDQAVQFVT EKRKASISGV QRQFRIGYNR AARIIEQMEA
QGIVSEQGHN GNREVLAPPP FD
