ID A0A397LJJ4_9FLAO Unreviewed; 795 AA.
AC A0A397LJJ4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=S-DNA-T family DNA segregation ATPase FtsK/SpoIIIE {ECO:0000313|EMBL:RIA09451.1};
GN ORFNames=OE09_1289 {ECO:0000313|EMBL:RIA09451.1};
OS Flavobacteriaceae bacterium MAR_2010_72.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250029 {ECO:0000313|EMBL:RIA09451.1, ECO:0000313|Proteomes:UP000265779};
RN [1] {ECO:0000313|EMBL:RIA09451.1, ECO:0000313|Proteomes:UP000265779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2010_72 {ECO:0000313|EMBL:RIA09451.1,
RC ECO:0000313|Proteomes:UP000265779};
RA Teeling H.;
RT "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT Genomic & Taxonomic Observatory).";
RL Submitted (AUG-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}.
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:RIA09451.1}.
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DR EMBL; QXCW01000002; RIA09451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397LJJ4; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000265779; Unassembled WGS sequence.
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:UP000265779};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 441..645
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 458..465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 795 AA; 88165 MW; 4D835E7D478EA7FF CRC64;
MAKKKTKTKS NTTSKLKKPK FKLSSQQKLI FGSLLIIIGI LLFIAFLSFF FTGKADQSTL
TELTSRDIKA ENWLNKLGAW VSDLFITKGF GIASFIFAGL LFLTGVYITL DINKTRLRKH
WIWGTLIAIW LSIFFGFFAN AYDALGGTIG FEMNSFFQDY MGKIGTALLL LFGLITYLAI
RFKVTGQSFV NLFRRAQNDI SSDFDTDGAS DSDQNMALDN NLTAEAEAIK SAFDLNVEHA
KPTIEKHSTR EQPSTPLKVE VPSDENELAM EVEETKEEVS ETDNLSNKLV EDFGQFDPTL
ELSKYQFPPL DLLNKYDAEG ITINQEELEE NKNRIVETLG NYNIGISNIK ATIGPTVTLY
EIVPNAGIRI SKIKNLEDDI ALSLSALGIR IIAPIPGKGT IGIEVPNKNA TIVSMRSVIA
AQRFQKSEME LPIAFGKTIS NETFVVDLAK MPHLLMAGAT GQGKSVGLNA VLTSLLYKKH
PAEVKFVLVD PKKVELTLFN KIERHYLAKL PDSEEAIITD NTKVINTLNS LCIEMDNRYE
MLKNAMCRNI KEYNEKFKAR KLNPNEGHQF LPYIVLVVDE FADLIMTAGK EVETPIARLA
QLARAIGIHL IIATQRPSVN VITGIIKANF PARIAFRVTS KIDSRTILDG SGADQLIGRG
DMLFTQGNDI IRIQCAFVDT PEVDKITEFI GSQKAYPEAY LLPEYVGEES GTSLDIDISD
RDQLFREAAE VIVTAQQGSA SLLQRKLKLG YNRAGRLIDQ LEAAGIVGGF EGSKARQVLI
PDLAALDKHL ENEGI
//