ID G8TJQ1_NIAKG Unreviewed; 846 AA.
AC G8TJQ1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Cell division FtsK/SpoIIIE {ECO:0000313|EMBL:AEW00798.1};
GN OrderedLocusNames=Niako_4540 {ECO:0000313|EMBL:AEW00798.1};
OS Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS GR20-10).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=700598 {ECO:0000313|EMBL:AEW00798.1, ECO:0000313|Proteomes:UP000005438};
RN [1] {ECO:0000313|EMBL:AEW00798.1, ECO:0000313|Proteomes:UP000005438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC {ECO:0000313|Proteomes:UP000005438};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Niastella koreensis GR20-10.";
RL Submitted (DEC-2011) 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}.
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DR EMBL; CP003178; AEW00798.1; -; Genomic_DNA.
DR AlphaFoldDB; G8TJQ1; -.
DR STRING; 700598.Niako_4540; -.
DR KEGG; nko:Niako_4540; -.
DR PATRIC; fig|700598.3.peg.4649; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_9_10; -.
DR Proteomes; UP000005438; 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 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, ECO:0000313|EMBL:AEW00798.1};
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 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 493..697
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 510..517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 846 AA; 93788 MW; 019A11D63A332484 CRC64;
MPMANRLKAD KAEKKKPAKS DSFKPEKEAQ VTVKQLVKDE RTHKIAGAFS ILISLFLFIA
FASYLFTWKE DQDKVFRGAA ILLPGEDVKT TNLLGNLGAY ISHLFFYKGF GAASFMFCSL
FFVIGVNALL GAKVFNLWRN VRYVIVSLLF FSVVLAFIFR GGAFAWGGAV GNMGSDWLVR
MIGSVGTAAL LLLGGLAYVI WRFNPVFKAP TLSKPKPAEP VKEVVPVLAK EDKETPVVKP
LGNKLKEGLG VLKKSPLTEP EEEPMDLQLV EKDGEGDEAP WDEEVEEMEE DVEEAPVEVT
PVIGKNGRNK KPDPAQLELE IKAYPEVDQP EVPIEEPKIE KVISQEPYDP SLELRDYKFP
SLELLELHGS ERIIQDPQEL ETNKNQIINT LKNYDIEIQK ISATVGPTVT LYEIVPAAGV
RISRIKNLED DIALSLAALG IRIIAPIPGK GTVGIEVPNV KKTVVSMRSM LSSEKFQNNS
FSLPIAIGKK IDNENFIVDL TTMPHLLMAG ATGQGKSVGL NAILVSLLYK KHPSQIKLVL
VDPKKVELSL YRHIETHFLA KLPGEDEAII TDTKKVIHTL NALCIEMDNR YDLLKEAGAR
NIREYNEKFI KRKLNPQKGH QFLPFIVLVV DEFADLIMTA GKEVEMPIAR LAQLARAVGI
HLIIATQRPS VNIITGTIKA NFPVRIAFKV SSKIDSRTIL DAGGAEQLIG KGDMLISYNG
EITRLQCAFV DTPEVDSICD FIGTQEGYPQ AFFLPEYVDE KQFEGKELNL EDRDTLFESA
ARMIVNSQMG STSLLQRRMK LGYNRAGRLM DQLEAAGIVG PSQGSKARDV LVKTEADLEM
LLNDIG
//
