ID A0A2V4MZS9_9ACTN Unreviewed; 912 AA.
AC A0A2V4MZS9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:PYC76967.1};
GN ORFNames=C7C46_20830 {ECO:0000313|EMBL:PYC76967.1};
OS Streptomyces tateyamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=565073 {ECO:0000313|EMBL:PYC76967.1, ECO:0000313|Proteomes:UP000248039};
RN [1] {ECO:0000313|EMBL:PYC76967.1, ECO:0000313|Proteomes:UP000248039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21389 {ECO:0000313|EMBL:PYC76967.1,
RC ECO:0000313|Proteomes:UP000248039};
RA Schwalen C.J., Hudson G.A., Mitchell D.A.;
RT "Bioinformatic expansion and discovery of thiopeptide antibiotics.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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. Required for activation of the Xer recombinase, allowing
CC activation of chromosome unlinking by recombination.
CC {ECO:0000256|ARBA:ARBA00024986}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PYC76967.1}.
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DR EMBL; PYBW01000078; PYC76967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4MZS9; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000248039; Unassembled WGS sequence.
DR GO; GO:0016020; C: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: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; 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; 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:0000313|EMBL:PYC76967.1};
KW Cell division {ECO:0000313|EMBL:PYC76967.1};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000248039};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 110..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 563..763
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 580..587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 912 AA; 95696 MW; 9608A9DC02BFBC54 CRC64;
MATRTSGSAA RNSSSGAAKK AAPAKKPAAR KSAAKASAAK PPAPKAPAKK ATARRTAAPR
PAAAPPAARP PILFRAVRAC WLGVAHSVGA VFRGFGDGAK GLHPHHRKDG LGLLLLALAL
VTAAGTWFSP QGWLGAAATS VVSGLFGRLD VLVPLLLAGM AVRLMRHPEV PEANGRIVIG
LSTLVVGVLG LVHIGCGAPG MQGGASRIRA AGGILGWAAS TPMMAAAGPP LAVPLLLLLA
FFGLLVVTAT PVNKIPERVR LLGVRLGVVE PGPLDELDQE WDTGGREYST EPPEDADPEA
LPYTVDEEQP EDELGARRRK RGRRRPAEQR LPAAAPDGFP AEPFQTRDLA AGVAADLDGA
LAYGVPASPA VASMMHQVQD RTAAPEESSV PPARTPAATD TAPTDTAPPG HSPAPPRMEQ
LQLLSGSGYA LPPLDLLERG GPAKARSALN DEVVAQLTAT FAEFKVDAKV TGFTRGPTVT
RYEVELGPAV KVERITALAK NIAYAVASPD VRIISPIPGK SAVGIEIPNR DREMVNLGDV
LRSRSAAEDT HPMVVGMGKD VEGHTVLANL AKMPHILVAG ATGAGKSSCI NCLITSVLAR
ATPDEVRMVL VDPKRVELTA YEGIPHLITP IITNPKKAAE ALQWVVREMD LRYDDLAAFG
FRHVDDFNAA VRAGKVTAPL GSERELTPYP YLLVIVDELA DLMMVAPRDV EDSVVRITQL
ARAAGIHLVL ATQRPSVDVV TGLIKANVPS RLAFATSAMA DSRVILDQPG AEKLIGKGDA
LFLPMGASKP VRMQGAFVTE AEIAAVVQHC KDQLSAVYRD DVTVSGGPKK EIDEEIGDDL
DLLIQAAELV VSSQFGSTSM LQRKLRVGFA KAGRLMDLME SRGIVGPSEG SKARDVLVKP
DELDGVLATI RG
//
