FTSK_VIBPA
ID FTSK_VIBPA Reviewed; 1028 AA.
AC Q87QP4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=VP1105;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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; BA000031; BAC59368.1; -; Genomic_DNA.
DR RefSeq; NP_797484.1; NC_004603.1.
DR RefSeq; WP_005489025.1; NC_004603.1.
DR AlphaFoldDB; Q87QP4; -.
DR SMR; Q87QP4; -.
DR STRING; 223926.28806092; -.
DR EnsemblBacteria; BAC59368; BAC59368; BAC59368.
DR GeneID; 1188610; -.
DR KEGG; vpa:VP1105; -.
DR PATRIC; fig|223926.6.peg.1047; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_0_2_6; -.
DR OMA; SWLTIVD; -.
DR Proteomes; UP000002493; Chromosome 1.
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..1028
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098317"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..1028
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 669..882
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 422..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 689..694
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1028 AA; 113058 MW; 526EAF3B2C95EE8C CRC64;
MFKENAKKVE TIIKTSEEPQ SSRLNGFQRL KECCFIVGVL SSVLLAVALF TFSPADPSWS
QTAWGGEIDN AGGLFGAWLA DTLFFTFGSL AYPIPFLLAA AAWVICRKRG EDEPIDFMLW
GTRLLGLTVL IMTSCGLADI NFDDIWYFSS GGVVGDVLSS LALPTLNVLG TTLVLLFLWG
AGFTLFTGIS WLNIVEWLGD RSLAVLAAIA NKFRGSEQET LEPQLDEFVE DKVSTKHVED
DQQDDETLPH LTAYEVEEPK EKAAVHEYPI YMPQAKSETS AVKPTPEPQP QRVAAVNATP
TYVEPEPQLK AVSTDNVDPM VERTKQLNVT IEELEAAAQQ ADDWASEEQT SQSYADTNAV
YQEQVQAKHE EVVEHDTPQL ESSYAEYAQF AAQQEQQLHV EPTPHEEPVI DTRALDDITD
HAEPSEHIEP TISDFDVVDE EETYVAPQPQ SRSPEPQPMV QPQSVSQIQP EQAPEPSVAF
EPAPQEVEVE EVQDGDQDVA AFQSMVSSAQ AKVAATQNPF LMKQEQNLPV PEEPLPTLEL
LYHPEKRENF IDREALEQVA RLVESKLADY KIKADVVGIY PGPVITRFEL DLAPGVKVSR
ISGLSMDLAR ALSAMAVRVV EVIPGKPYVG LELPNMSRQT VYLSDVISSP QFEQAKSPTT
VVLGQDIAGE AVIADIAKMP HVLVAGTTGS GKSVGVNVMI LSMLYKASPE DLRFIMIDPK
MLELSIYEGI PHLLAEVVTD MKDASNALRW CVGEMERRYK LMSALGVRNV KGFNEKLKMA
AEAGHPIHDP FWQEGDSMDT EPPLLEKLPY IVVVVDEFAD LMMVVGKKVE ELIARLAQKA
RAAGIHLILA TQRPSVDVIT GLIKANIPTR VAFTVSTKTD SRTILDQGGA ESLLGMGDML
YLPPGSSHTI RVHGAFASDD DVHAVVNNWK ARGKPNYIDE IISGDQGPES LLPGEQMESD
EEMDPLFDQV VEHVVQSRRG SVSGVQRRFK IGYNRAARIV EQLEAQGIVS APGHNGNREV
LAPAPPKD
