ID B7KZJ0_METC4 Unreviewed; 871 AA.
AC B7KZJ0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN OrderedLocusNames=Mchl_2377 {ECO:0000313|EMBL:ACK83222.1};
OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS extorquens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=440085 {ECO:0000313|EMBL:ACK83222.1, ECO:0000313|Proteomes:UP000002385};
RN [1] {ECO:0000313|Proteomes:UP000002385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT CM4.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACK83222.1, ECO:0000313|Proteomes:UP000002385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RX PubMed=22887658; DOI=10.1128/JB.01009-12;
RA Marx C.J., Bringel F., Chistoserdova L., Moulin L., Farhan Ul Haque M.,
RA Fleischman D.E., Gruffaz C., Jourand P., Knief C., Lee M.C., Muller E.E.,
RA Nadalig T., Peyraud R., Roselli S., Russ L., Goodwin L.A., Ivanova N.,
RA Kyrpides N., Lajus A., Land M.L., Medigue C., Mikhailova N., Nolan M.,
RA Woyke T., Stolyar S., Vorholt J.A., Vuilleumier S.;
RT "Complete genome sequences of six strains of the genus Methylobacterium.";
RL J. Bacteriol. 194:4746-4748(2012).
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.
CC {ECO:0000256|ARBA:ARBA00024784}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000256|ARBA:ARBA00025923}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001298; ACK83222.1; -; Genomic_DNA.
DR RefSeq; WP_015950838.1; NC_011757.1.
DR AlphaFoldDB; B7KZJ0; -.
DR KEGG; mch:Mchl_2377; -.
DR HOGENOM; CLU_001981_6_2_5; -.
DR Proteomes; UP000002385; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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 CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.30.980.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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 PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
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; SM00382; AAA; 1.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:ACK83222.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 497..716
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 188..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514..521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 871 AA; 93197 MW; E1906B6C0021E7B4 CRC64;
MRSLRRSASP YDTFVDSLRP FLAKRLTECG GLILFTGAVA LTVALATWSI NDPSLNHATD
QRAHNVLGRP GAVVADLAMQ LLGLGSIALA LPPALWGVRL MRERDLPHGG LRIVLWFVGV
LCASAVASAL PPTDRWPLPT GMGGVAGDAL LAGTRMLVGP LAHFAGFLFA ASAILSLTAA
CRVTKPDFEE DEEGPYGAAR PAPRSGRAST HEERHDADEP SLGILSLGAL AQAVMRGRAS
LRTRLESWQA PADEAEGLAY AGASPALAAR RAFADSDEAP WAPQARERAD VSGRREPQFD
SEEDDSDEAP ARAVPQRAAP SAAGAETTAD ELPTRVSRPL PQAPAARPRP AEPRPEAGEY
RLPALELLAR PREAAPGSEV SAEALEQNAT MLEATLQDFG VRGDILAVRP GPVVTLYELE
PAPGTKSSRV IALADDIARS MSAVSARVAV VPGRNAIGIE LPNAKRETVF LRELLASEDF
VETKQKLALC LGKNIGGEPI IADLARMPHL LVAGTTGSGK SVAINTMILS LLYRLKPEEC
RLIMVDPKML ELSVYDGIPH LLSPVVTDPK KAVIALKWAV REMEERYKKM SKVGVRNIDG
FNARLEEARA RGETLTRTVQ TGFDRSTGEA VYEDEVMDLN PLPYIVIVVD EMADLMMVAG
KDIEGAIQRL AQMARAAGIH LIMATQRPSV DVITGTIKAN FPTRISFQVT SKIDSRTILG
EMGAEQLLGQ GDMLFMAGGG RTTRVHGPFC SDSEVETVVA HLKRQGRPSY LEAVTAEEGE
IPAGGPASED GPVFDAGQFG GGGESGDLYE QAVAVVLRDK KASTSYIQRR LQIGYNRAAS
LMERMETEGL VGPANHAGKR EILVEPEPQA Y
//
