ID I0IH37_PHYMF Unreviewed; 952 AA.
AC I0IH37;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Putative DNA translocase FtsK {ECO:0000313|EMBL:BAM04575.1};
GN Name=ftsK {ECO:0000313|EMBL:BAM04575.1};
GN OrderedLocusNames=PSMK_24160 {ECO:0000313|EMBL:BAM04575.1};
OS Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / FYK2301M01).
OC Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae; Phycisphaera.
OX NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM04575.1, ECO:0000313|Proteomes:UP000007881};
RN [1] {ECO:0000313|EMBL:BAM04575.1, ECO:0000313|Proteomes:UP000007881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01
RC {ECO:0000313|Proteomes:UP000007881};
RA Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Phycisphaera mikurensis NBRC 102666.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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; AP012338; BAM04575.1; -; Genomic_DNA.
DR RefSeq; WP_014437788.1; NC_017080.1.
DR AlphaFoldDB; I0IH37; -.
DR STRING; 1142394.PSMK_24160; -.
DR GeneID; 80849528; -.
DR KEGG; phm:PSMK_24160; -.
DR PATRIC; fig|1142394.8.peg.2497; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_0; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000007881; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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; 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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000007881};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 539..743
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..944
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 556..563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 952 AA; 101311 MW; 2EDD071F1FCA4BBD CRC64;
MAETSVSIRR SAPRKTTATR RKPATRSRAK APPKLTAAQK RHRAAAFLAV CWSVAALAWV
LAGLALGSHD PADAPAHALG VTNVQPNNWV GAAGAAFSHR AVLVLGPGVW VAYAAAGLWL
AATAAGRRPD QSILRLAGVG LMTAAGAGLA SVGHASFSAT GPVTPEGPGG LLGLFLQDEL
VPRFAGLGAM LILGVVFWVG AVLAADRWVL LIPRLAGAAL LKALNASRVT LPPVATAAGN
AAQTAVGAAQ GLRFPRIGVD AGDPAPPARA NDVDDDFRPS PAGGDDGEDP EEDHEEDEPA
APRRSLARYL PKRKPAEPEP EDSDEEDVGA PAAYVASKKA AVPGAPAEGE PPPLDAAALK
AKMAKLPVNF APKIDAASAA APEPGDGAGL DAGENEPVDL SGYRFPGVDL LVEPEGSFRE
HLESYIRRQG EALQNALNEF GIQAEVVNVD SGPVITLFEI RLAPGTKVSR ISAIDSDVAR
ALKAPNIRVV ANMAGKDTVG IEVPNEEKER VRLRELLTAN PGALEKMKLP MFLGKDASGN
PLIQDLNAMP HMLIAGTTGS GKSVCMNSII MSFLLTKKPD ELKLVLVDPK MVEMSQFKSI
PHLMCPVVTE MSKAAAILEW AVTKMDERYE LLAEAGVRDI ASYNELGIEE LIERMEPASD
EEESRIPRKL PYLVFIIDEL ADLMMTNKEV ESHIVRIAQK ARAVGMHLIL ATQRPSANVV
TGLIKSNMPC RVCMKVNSGM DSRIILDAKG GELLLGHGDM LFVSPRSSEL VRAQGTLVDD
HEIRKCTRFL KEISSQSFEQ SLVQLKKVDE EEGEEQAFAD RDPLFDKAVE VVLETQRGSV
SLLQRKLTIG YARSSRIIEQ MERYGIIGGH KTAQARKVLV TPEEWEAMIE LARKEAAGGE
SADGVGSDDA EQEVPEVATA AGSSDSDGWE EADEADEEDG GWSDAEASID TR
//