ID A0A386HM47_9BACT Unreviewed; 849 AA.
AC A0A386HM47;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:AYD46978.1};
GN ORFNames=D6B99_04730 {ECO:0000313|EMBL:AYD46978.1};
OS Arachidicoccus soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Arachidicoccus.
OX NCBI_TaxID=2341117 {ECO:0000313|EMBL:AYD46978.1, ECO:0000313|Proteomes:UP000266118};
RN [1] {ECO:0000313|EMBL:AYD46978.1, ECO:0000313|Proteomes:UP000266118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIS59-12 {ECO:0000313|EMBL:AYD46978.1,
RC ECO:0000313|Proteomes:UP000266118};
RA Weon H.-Y., Kwon S.-W., Lee S.A.;
RT "Arachidicoccus sp. nov., a bacterium isolated from soil.";
RL Submitted (SEP-2018) 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; CP032489; AYD46978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A386HM47; -.
DR KEGG; ark:D6B99_04730; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000266118; 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};
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:UP000266118};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 495..699
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 512..519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 849 AA; 94054 MW; 75BCCCF5190DB31F CRC64;
MPNNLKTNKS AIPSPDKLNP EKEVNVTVSE IVRDERTYKI TGAILLLIGF FLFISFASYL
FTWQEDQDKV MSFGVKIFST SDMKVSNLFG VLGAYTSHNL MYNGFGVASF LLCTSFFVAG
VNFLFGKKVF SLRRNIKYVV AGLIVLSTTF AFLNMELLKT GFSWGGAAGE LVCEWLLKWI
GTLGTICAIL LILGIYLIWR FDPVFSLHIF SKREKKIAVV DSEMEEEGDV APENEGAQLF
VDSQVAAGNQ LKNKKSKGVS VILPEFDVED DLALSVDEKN EEEIPSINEV FAAEEEKEKL
KPLEAKATRA IVPNPENMPL EIKPEVEEIP SEIIVNTDAP QAQVLAQSNY EPTLDLSNYK
YPSIELLDIH GTEKSIHDPE ELEQNKNQII STLKNYDIHI QRISATVGPT VTLYEIVPAP
GVRISRIKNL EDDIALSLAA LGIRIIAPIP GKGTIGIEVP NINKTIVSMR GLIASDKFQN
NNFSLPIAIG KKINNENFIV DLASMPHLLM AGATGQGKSV GVNALLVSLL YKKHPSQLKF
VLVDPKKVEL SLYRTIEHHF LAKLPGEEEA IITDTKKVVT TLNALCIEMD NRYDLLKEAG
CRNIKEYNEK FVKRRLNPQK GHQFLPFIVL VIDEFADLIM TAGKEIEMPI ARLAQLARAV
GIHLIIATQR PSVNIITGTI KANFPARIAF KVSSKIDSRT ILDAGGAEQL IGKGDMLISY
NGEITRLQCA FVDTPEVDKV CDFIGEQQGY PEAFLLPEYV DEKELAASGG NDLTDRDPLF
EDAAKLIVQN QVGSTSLIQR RMKLGYNRAG RLMDQLEMAG IVGSNQGSKA RDVLIKTDAD
LQYLLDNIP
//