ID A0A0G1KBI6_9BACT Unreviewed; 1208 AA.
AC A0A0G1KBI6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Cell division FtsK/SpoIIIE {ECO:0000313|EMBL:KKT45149.1};
GN ORFNames=UW34_C0004G0012 {ECO:0000313|EMBL:KKT45149.1};
OS Parcubacteria group bacterium GW2011_GWA2_44_15.
OC Bacteria.
OX NCBI_TaxID=1618831 {ECO:0000313|EMBL:KKT45149.1, ECO:0000313|Proteomes:UP000034891};
RN [1] {ECO:0000313|EMBL:KKT45149.1, ECO:0000313|Proteomes:UP000034891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT45149.1}.
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DR EMBL; LCHY01000004; KKT45149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KBI6; -.
DR PATRIC; fig|1618831.3.peg.149; -.
DR Proteomes; UP000034891; 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:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 3.30.980.40; -; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR003586; Hint_dom_C.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR01443; intein_Cterm; 1.
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; 2.
DR Pfam; PF14890; Intein_splicing; 1.
DR Pfam; PF14528; LAGLIDADG_3; 2.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SMART; SM00305; HintC; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50901; FTSK; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:KKT45149.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
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}; Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 548..684
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 837..1048
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 184..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 909..936
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 202..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 857..864
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1208 AA; 134150 MW; 3EB4410583197A2A CRC64;
MSKNTRNNID TGKKGFFRIW RDIPEGTKQG ILAIIFFVVS VLFTLASFGK AGFVGETTYR
WFKFLLGFGY FLVPIVFVML GITFLKTLKH SFPTVKIASS ILFLLAGLGI IEVNIPGKGG
AIGSLISTPL LKLFDTYASI IVLGAIFVIS IIIIFETEFT VEPLIRWWKK LRFKGADRNE
TLTDTASDED WLPPPTEEIN NATPEEKQKL QEKVDRKNTA KKDGRENGIG QSEEIAFNKK
TSPSMFKNAG KVFSPPPLSL LERDKGKPVV GDINANKNII KRTLQNFGIN VEMDEISIGP
SVTRYSLKPA EGVKLSRIVA LQNDLSLALA AHPLRIEAPI PGKSLVGIEI PNTTKSIVGL
ATLLASEEYQ KSEKSLLISL GKGISGKSHF ANLAKMPHLL IAGTTGSGKT CGKDTYVFSE
KGVLTFEELC PLPLNSEIDY SLRVATRDGL ETTSKNYNNG ICDFYKITTA EGLSIEVTEE
HPLWVIRDGA MAWQNGGNIR IGEYVAISRG SKLFGEDKQI NFTPALNKTN KAREIKTPTR
MTPKLGLFMG LLTADGGLTV KNRVVYTQAN KEVLDVYVEL LRNLFDITAP IIAKSGSSDK
AKDIVVNSKH LKGFLTHLGL KPVGAREKEI PKSIRESGPE VIKSFIRGLI RNDGHISALK
GLEITLATEK LLRQLQIVLL NFGIVSSVHS KKVKNYPENN YWRLAVYGGE FVAYAKEIGF
LTDEEKEKAK LLLALRRNTN KNIIPTLKSV LKKLSLTYRG IFARLTNKGW NYQQGALVPK
YAFRSLASYS SGLRNPSYET LEKILNFYGS LAESDDYKKV SEIHKDNFYW AKVVKIEKTV
GEGYDFEVPG SNSFVGNGFV NHNSVTIHTI ITSLLFRNSV ENIKFIMIDP KRVELTLYNK
IPHLLTPVIT EAKKAILALK WAAKEMERRY DILESESVRD VESYHKNVLE PELKKLEKQS
AGESEADMKM PELMPYIIIV IDELADIMST YPRELEAAIV RLAQMSRAVG IHLILSTQRP
SVNVITGLIK ANIPGRIALQ VSSQIDSRTI LDTGGAEKLL GAGDMLFLGS EMSKPQRIQS
AYISETEVKK VVSYLKNNYD DGVPSELNLT PEAVADKNAI FEASFGDDED VDDDLYEQAR
EEVIKAGKAS TSYIQRKLRV GYARAARLVD LLQERGIIGP ADGARPREVI GGKMDTESQT
EMEEEPHQ
//
