ID A0A1I2E0H1_9BACT Unreviewed; 855 AA.
AC A0A1I2E0H1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SFE86083.1};
GN ORFNames=SAMN05518672_11177 {ECO:0000313|EMBL:SFE86083.1};
OS Chitinophaga sp. CF118.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1884367 {ECO:0000313|EMBL:SFE86083.1, ECO:0000313|Proteomes:UP000199596};
RN [1] {ECO:0000313|EMBL:SFE86083.1, ECO:0000313|Proteomes:UP000199596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF118 {ECO:0000313|EMBL:SFE86083.1,
RC ECO:0000313|Proteomes:UP000199596};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOMK01000011; SFE86083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2E0H1; -.
DR STRING; 1884367.SAMN05518672_11177; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000199596; 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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 502..706
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 519..526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 855 AA; 95811 MW; 6E87AA4D2F844F79 CRC64;
MSRNKLKTEK PESKKPRGDD PNVLKQEKEA EVKVKELVKD ERTHKVMGVI YLLLSLYCFI
AFTSYLFTWE DDQDKVFRYA SSVLFMDDLK VENLLGRLGA FVSHWFIYGG FGVAAYLFCY
LFFILGVNFI VGRRVFRIWR NIKYILFGLL FISTAAAFVT GMAGFPWGGA LGDAVSKWIT
GFLGTAGAAL LLLVAGFSWV IWKYNLDFKW LMERKPKKIL VPAGVAEAVV AVENIKDGKR
RNGLKDNGVV VIPPAAETDE LPEMQLVVKN EKITVVPPAY VPPVVDEDEE LEEEEEEEEE
VGPLLYIEET VEQTSSRKKN RLPEDVPFEL KPPVEEAEDD IAPDEQPATG PVQLDPYDPI
LDLRDYKYPT LELLDNHGTE KIVQDVTELE RNKNQIIDTL KNYDISIQKI SATVGPTVTL
YEIVPAAGVR ISRIKNLEDD IALSLSALGI RIIAPIPGKG TIGIEVPNVK KSIVSLRNLL
ASEKFQQSTM DLPIAIGKKI DNENFIADLA KMPHLLMAGA TGQGKSVGIN TLLVSLLYKK
HPSQLKFVLI DPKKVELSLY KLIEKHFLAK LPGEEDAIIT DIKKVIHTLN ALCIEMDIRY
DLLKEAGTRN IREYNVKFTQ RRLNPEKGHR YLPFIVLVID EFADLIMTAG KEVEMPIARL
AQLARAIGIH LIIATQRPSV NIITGTIKAN FPARIAFKVS SKIDSRTILD IGGSEQLIGQ
GDMLVSFNGE LVRLQCAFVD TPEVERVAEF IGRQRGYPEA FLLPEYVDDK DMEGKEISLQ
DRDTLFEEAA RIIVQNQQGS TSLLQRRMKL GYNRAGRLMD QLEAAGIVGP NMGSKARDVH
VKTESDLEEI LDSLG
//
