FTSK_PSEU2
ID FTSK_PSEU2 Reviewed; 801 AA.
AC Q9Z3U1; Q4ZRL1;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=Psyr_3179;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kisncherf T.G., Hirano S.S., Willis D.K.;
RT "A transposon insertion in the ftsK/spoIIIE gene impairs in planta growth
RT and lesion forming abilities in Pseudomonas syringae pv. syringae B728a.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; AF095845; AAC98298.1; -; Genomic_DNA.
DR EMBL; CP000075; AAY38211.1; -; Genomic_DNA.
DR RefSeq; WP_003405080.1; NC_007005.1.
DR RefSeq; YP_236249.1; NC_007005.1.
DR AlphaFoldDB; Q9Z3U1; -.
DR SMR; Q9Z3U1; -.
DR STRING; 205918.Psyr_3179; -.
DR EnsemblBacteria; AAY38211; AAY38211; Psyr_3179.
DR KEGG; psb:Psyr_3179; -.
DR PATRIC; fig|205918.7.peg.3244; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_6; -.
DR OMA; YKAEARD; -.
DR Proteomes; UP000000426; 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..801
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098281"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 441..653
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 715..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 461..466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 801 AA; 87657 MW; 84D2645B57C1006D CRC64;
MKKSTPAPSA VPLWRQQLHY RLKEGALIAF GALCLYLMMA LLTYDQSDPG WSHTSSNAAQ
VQNAAGRAGA FCADILFMIL GYFAYIFPLL LAIKAWQVFR HRHEPWQWSG WLFSWRLIGL
VFLILAGAAL AHIHFHFSAG FPGSAGGVLG EVLGDLAKKA LNIQGSTLLF IALFLFGLTV
FTDLSWFKVM DVTGKITLDL FELFQGAANR WWTARAERKQ MVAQLREVDM RVNDVVAPVA
PDRREQAKAR ERLVEREASL SKHMTEREKH VPAVIAPAPS KPVEPSKRVM KEKQAPLFVD
SAVEGTLPPI SILDPAEKKQ LNYSPESLAA VGHLLEIKLK EFGVEVSVDS IHPGPVITRY
EIQPAAGVKV SRISNLAKDL ARSLAVTSVR VVEVIPGKTT VGIEIPNEDR QIVRFSEVLS
TPEYDNAKSP VTLALGHDIG GKPVITDLAK MPHLLVAGTT GSGKSVGVNA MILSILFKSG
PEDAKLIMID PKMLELSIYE GIPHLLCPVV TDMKDAANAL RWSVAEMERR YKLMAKMGVR
NLSGFNQKVK EAQDAGEPLA DPLYKRESIH DEAPLLSKLP TIVVVVDEFA DMMMIVGKKV
EELIARIAQK ARAAGIHLIL ATQRPSVDVI TGLIKANIPT RMAFQVSSKI DSRTIIDQGG
AEQLLGHGDM LYMPPGTSLP IRVHGAFVSD EEVHRVVEAW KLRGSPDYND DILAGVEEPG
SGFDGGSGEG SEDSESDALY DEAVKFVLES RRASISAVQR KLKIGYNRAA RMIEAMEMAG
VVTSMNTNGS REVLAPGPVR D