FTSK_LISMO
ID FTSK_LISMO Reviewed; 757 AA.
AC Q8Y7A3;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=lmo1386;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(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. Required for activation of the Xer recombinase, allowing
CC activation of chromosome unlinking by recombination (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Located at the septum. {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 form the DNA pump, and the gamma
CC subdomain is a regulatory subdomain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; AL591979; CAC99464.1; -; Genomic_DNA.
DR PIR; AB1248; AB1248.
DR RefSeq; NP_464911.1; NC_003210.1.
DR RefSeq; WP_010990110.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y7A3; -.
DR SMR; Q8Y7A3; -.
DR STRING; 169963.lmo1386; -.
DR PaxDb; Q8Y7A3; -.
DR EnsemblBacteria; CAC99464; CAC99464; CAC99464.
DR GeneID; 987830; -.
DR KEGG; lmo:lmo1386; -.
DR PATRIC; fig|169963.11.peg.1424; -.
DR eggNOG; COG1280; Bacteria.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_6_9; -.
DR OMA; FGEWYML; -.
DR PhylomeDB; Q8Y7A3; -.
DR BioCyc; LMON169963:LMO1386-MON; -.
DR Proteomes; UP000000817; 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; IPR003593; AAA+_ATPase.
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; 1.
DR SMART; SM00382; AAA; 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 membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..757
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098269"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 423..619
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 443..448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 757 AA; 83551 MW; F6B88B6B1E929BD2 CRC64;
MATQKKKTSG RKKSSTRSKK KQSASFRLEI TGVILIAIGV IGLLQLGFVG RGFFALAEMF
VGLLSYVLLA GSVILGGYMV IRRKMPHLFS KRLVGIYLIV LGFLTYIHMY FIIHNLGANA
SVVSSTWKLV LENLFRPNQV GFVGGGMIGA AITSITYFLL DRLGTNLIAV LLIIYGFSLV
SGISIRQFFS KIAEFVRYLF TKGKVATEKG KEVKAKRDKK KAEKIVDVEP DEVIDVIEPL
QEEKTPPIIS NFSSKVEQEK APVEEKISQK EQDLEMFQQE SFENEIYQLP PVDILAPAKV
TDQSKEYDQI KVNAKKLEDT FESFGVKAKI TQVHLGPAVT KYEVQPSVGV KVSKIVSLSD
DIALALAAKD IRIEAPIPGK SAIGIEVANQ NVAMVSLREV LENNPKNNPD EKLQIALGRD
ISGEAMMANL DKMPHLLVAG ATGSGKSVCI NGIITSILLR AKPHEVKMMM IDPKMVELNV
YNGIPHLLAP VVTNPKKAAQ ALQKVVAEME RRYDLFSHTG TRNMQGYNDY VKKHNELNEE
KQPELPFIVV IVDELADLMM VASNDVEDAI TRLAQMARAA GIHLIIATQR PSVDVITGVI
KANIPSRIAF AVSSSIDSRT ILDMGGAEKL LGRGDMLLLP VGSSKPTRIQ GAFLSDAEVE
DVVNYVISQQ KAQYSEEMIP DDIPEVEGEV TDELYHEAVE LVVEMQTASV SMLQRKFRIG
YNRAARLIDE MEQRGVVGPH EGSKPRRVNV EVSPEHE
