FTSK_AZOBR
ID FTSK_AZOBR Reviewed; 631 AA.
AC O83045;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=DNA translocase FtsK;
DE Flags: Fragment;
GN Name=ftsK;
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=9720864; DOI=10.1046/j.1365-2958.1998.00938.x;
RA de Zamaroczy M.;
RT "Structural homologues PII and PZ of Azospirillum brasilense provide
RT intracellular signalling for selective regulation of various nitrogen-
RT dependent functions.";
RL Mol. Microbiol. 29:449-463(1998).
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; X92496; CAA63241.1; -; Genomic_DNA.
DR AlphaFoldDB; O83045; -.
DR SMR; O83045; -.
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; 3.40.50.300; -; 1.
DR InterPro; IPR025199; FtsK_4TM.
DR InterPro; IPR041027; FtsK_alpha.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13491; FtsK_4TM; 1.
DR Pfam; PF17854; FtsK_alpha; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 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..>631
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098235"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..>631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 478..>631
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498..503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT NON_TER 631
SQ SEQUENCE 631 AA; 67101 MW; 81CAB67411DE639D CRC64;
MARPASPRSG SGKSAGARPA GARTEKPPFF SPATRAFVVA RAREMAGFAL GVVGLVLMVI
LGSYNPADPS WNAVPAADVH IHNLFGRFGA HLADVLIQSL GWAAYLLALV PMMWGWRLSL
QKSVRHPLFR SVLAVWGVLM VAMFLAGMGT GSEDPLKSRP GGSFGGLLLD GVSRLLFGSP
GNPLVGTVAG VAGGLILFVA MGLSIREWAA SLRETAAGLA RLGRGARTGL SFVRDKGAEA
ARSAARQTGG LLRREPSLAT AEKTTAAPTL DDTPDEDGGA ITLRAAPRGR LSDSISVEPR
VEAKTRAVPV VTSPAGGKTK AADQGRPSKQ AALNLEEADG YELPPLDLLQ IVPTSVRGEK
VDEAALRENA VKLEGVLSDF GVRGEVQKVH PGPVVTLYEL EPAPGTKSSR VIGLADDIAR
SMSAVSVRVA VVPGRNVIGI ELPNAKRETV LLRELLAGDV FDKTAGKLLL ALGKDIGGQS
VVADLARFPH LLVAGTTGSG KSVAINTMIL SLLYRLPPDR CRFIMIDPKM LELSVYEGIP
HLLTPVVTDP KKAVVALKWT VREMEDRYRN MSKLGVRNIE GYNARLREAR ADGELLTRRV
QTGFDPDTGK PIFEEQPLDL KELPYIVVIV D
