ID A0A1G9C732_9CLOT Unreviewed; 762 AA.
AC A0A1G9C732;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:SDK47469.1};
GN ORFNames=SAMN05660472_01384 {ECO:0000313|EMBL:SDK47469.1};
OS Natronincola ferrireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Natronincola.
OX NCBI_TaxID=393762 {ECO:0000313|EMBL:SDK47469.1, ECO:0000313|Proteomes:UP000198718};
RN [1] {ECO:0000313|EMBL:SDK47469.1, ECO:0000313|Proteomes:UP000198718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18346 {ECO:0000313|EMBL:SDK47469.1,
RC ECO:0000313|Proteomes:UP000198718};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000256|ARBA:ARBA00025923}.
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; FNFP01000002; SDK47469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9C732; -.
DR STRING; 393762.SAMN05660472_01384; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000198718; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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; 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: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:UP000198718};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 428..615
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 445..452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 762 AA; 84173 MW; 52AE9559F67BD630 CRC64;
MSRKSKKTKE GFSSFKKEFN NEIYGIFIIA FGLILLTALH SSSSGKIGGG LKFLLMGLFA
NLALVLPYAI VFLGILVFID KPFWKELKGI LFFILIFLCF LVFKSLLDIN FIKEISQQGF
FYSIPTIFTK GTEGLGGGII GTAITYLLVN LFGQVGSYIV IIAILLISLI MYTKISIVGF
IVKLKVLINK ILVFIKSFIS RSLPLMKNNS NDISPKLEKD SGIPVVEDER ITIENNVDEK
IKILDYTVID NNYSEKENAI KEKEAKAQIS ISQDEPSVLG GNNYHQKEHI EYELPNSGLL
NEIDYIPNKE DKKKIVSKAR LLEETLKNFG VQAKVLQVSK GPTITRYELQ PSTGVKVSKI
VNLSDDIALN LAASAIRIEA PIPGKAAIGI EIPNEDITTV TLRELIDSEC YQSFSHSLPF
ALGKDISGAP IVTDISKMPH LLIAGATGSG KSVCINTLIL SLLYKSKPEK VRLLLIDPKV
VELNQYNGIP HLLIPVVTDA KKATSALNWA VQEMTQRYKI FGELGVKDIN GYNEKFEENP
LPYIVIIIDE LADLMLVAPN DVEDAICRLA QMARAAGMHL IIATQRPSVD VITGVIKANI
PSRIAFSVAS QADSRTILDM GGAEKLLGKG DMLFHPIGAS KPVRIQGAFV GEKEVERVVT
FIKEQIENPS YETEIVDKID NNSMIAEDIN CDELFDDALK IVVENQQASI SMLQRKLKIG
YNRAARLIDD MEARGIVGPH EGSKPRQVLV TQESLLAKAE NE
//
