FTSK_STRA3
ID FTSK_STRA3 Reviewed; 816 AA.
AC Q8E418;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=gbs1585;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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 difSL
CC recombination site, which is located within the replication terminus
CC region. Required for activation of the XerS 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD47244.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL766852; CAD47244.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000231576.1; NC_004368.1.
DR AlphaFoldDB; Q8E418; -.
DR SMR; Q8E418; -.
DR STRING; 211110.gbs1585; -.
DR EnsemblBacteria; CAD47244; CAD47244; CAD47244.
DR KEGG; san:gbs1585; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_6_9; -.
DR Proteomes; UP000000823; 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 Transmembrane; Transmembrane helix.
FT CHAIN 1..816
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098301"
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..816
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 475..671
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 726..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 495..500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 816 AA; 90682 MW; F96AA6278A9DA0C5 CRC64;
MVFMANKKKT KGKKTRRPTK AEIERQRAIQ RMITALVLTI ILFFGIIRLG IFGITVYNVI
RFMVGSLAYL FIAATLIYLY FFKWLRKKDS LVAGFLIASL GLLIEWHAYL FSMPILKDKE
ILRSTARLIV SDLMQFKITV FAGGGMLGAL IYKPIAFLFS NIGAYMIGVL FIILGLFLMS
SLEVYDIVEF IRAFKNKVAE KHEQNKKERF AKREMKKAIA EQERIERQKA EEEAYLASVN
VDPETGEILE DQAEDNLDDA LPPEVSETST PVFEPEILAY ETSPQNDPLP VEPTIYLEDY
DSPIPNMREN DEEMVYDLDD DVDDSDIENV DFTPKTTLVY KLPTIDLFAP DKPKNQSKEK
DLVRKNIRVL EETFRSFGID VKVERAEIGP SVTKYEIKPA VGVRVNRISN LSDDLALALA
AKDVRIEAPI PGKSLIGIEV PNSEIATVSF RELWEQSDAN PENLLEVPLG KAVNGNARSF
NLARMPHLLV AGSTGSGKSV AVNGIISSIL MKARPDQVKF MMIDPKMVEL SVYNDIPHLL
IPVVTNPRKA SKALQKVVDE MENRYELFSK IGVRNIAGYN TKVEEFNASS EQKQIPLPLI
VVIVDELADL MMVASKEVED AIIRLGQKAR AAGIHMILAT QRPSVDVISG LIKANVPSRI
AFAVSSGTDS RTILDENGAE KLLGRGDMLF KPIDENHPVR LQGSFISDDD VERIVGFIKD
QAEADYDDAF DPGEVSETDN GSGGGGGVPE SDPLFEEAKG LVLETQKASA SMIQRRLSVG
FNRATRLMEE LEAAGVIGPA EGTKPRKVLM TPTPSE
