ID A0A1G9DCZ9_9BACT Unreviewed; 832 AA.
AC A0A1G9DCZ9;
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:SDK61735.1};
GN ORFNames=SAMN05421823_10379 {ECO:0000313|EMBL:SDK61735.1};
OS Catalinimonas alkaloidigena.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Catalimonadaceae;
OC Catalinimonas.
OX NCBI_TaxID=1075417 {ECO:0000313|EMBL:SDK61735.1, ECO:0000313|Proteomes:UP000198510};
RN [1] {ECO:0000313|EMBL:SDK61735.1, ECO:0000313|Proteomes:UP000198510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25186 {ECO:0000313|EMBL:SDK61735.1,
RC ECO:0000313|Proteomes:UP000198510};
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; FNFO01000003; SDK61735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9DCZ9; -.
DR STRING; 1075417.SAMN05421823_10379; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000198510; 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:UP000198510};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 475..680
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 221..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..262
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 493..500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 832 AA; 91819 MW; FBBDC752C9F182D7 CRC64;
MAKNTYKKKE KEKRPRKNPF QGVARFFTDR RVHLSIGLLL LISAIFLGVA FISFLFTGAA
DQSVIESIRT TGVRPAGSEI ENWLGITGAW LSHLFMFRWL GISAFFLLPI LFGVGYQIVF
RRELVPLYRL INLCLFAAVW LSITIGSILL ATGHAEEWGQ LSGGIGYEWG LVFRQFLGLG
SFVLLAFALA VFVIFYFDIT HINAPHWKWA LRSDVSDQTA YNAQADLEEE EEEEEAPAAR
EPRRAAPPPP PEPMPEPEPE PEPAYAQFER EANVTPPPRP AASNRNGHEI PLDIDMGPAD
DEPEEEEEDG PSFTIEKPVE EPLAAAGEEA YDPTLDLASF QLPPVELLQE HSSGEHQVSS
DELEANKNRI VETLSNYGIG IASIKAAIGP TVTLYEIVPE AGVRISKIKN LEDDIALNLA
ALGIRIIAPI PGKGTIGIEV PNKNREIVSA RGVISTEKFL KSKAELPIVL GKNISNEVFV
TDLAKMPHLL MAGATGQGKS VGLNVLLTSL IYRKHPSQLK FVLVDPKKVE LSLFSKIERH
YLAMLPDGDE AIITDTKKVI NTLNSLCIEM DTRYDLLKDA GCRNLKEYNQ KFTQRKLNPE
KGHRYMPYIV LVIDELADLM MTAGKEVETP IARLAQLARA IGIHLVVATQ RPSVNVITGI
IKANFPARLS FKVTSKVDSR TILDTGGAEQ LVGMGDMLLS INSELTRLQC AFVDTPEVEA
VCDFVGQQRG YESAYLLPEY YGDDSGDSSK GDVDLADRDP MFADAARVIV AHQQGSTSLL
QRRLKLGYNR AGRLIDQLEA AGIVGPFEGS KAREVLIRDE VSLEQLLSNL DS
//
