ID A0A2W5WJ69_9MICO Unreviewed; 1457 AA.
AC A0A2W5WJ69;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Cell division protein FtsX {ECO:0000313|EMBL:PZR51569.1};
GN ORFNames=DNL40_15870 {ECO:0000313|EMBL:PZR51569.1};
OS Xylanimonas oleitrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Xylanimonas.
OX NCBI_TaxID=2607479 {ECO:0000313|EMBL:PZR51569.1, ECO:0000313|Proteomes:UP000248783};
RN [1] {ECO:0000313|EMBL:PZR51569.1, ECO:0000313|Proteomes:UP000248783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PW21 {ECO:0000313|EMBL:PZR51569.1,
RC ECO:0000313|Proteomes:UP000248783};
RA Nagkirti P., Shaikh A., Gowdaman V., Engineer A.E., Dagar S.,
RA Dhakephalkar P.K.;
RT "Whole genome sequencing of a novel hydrocarbon degrading bacterial strain,
RT PW21 isolated from oil contaminated produced water sample.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:PZR51569.1}.
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DR EMBL; QKWH01000020; PZR51569.1; -; Genomic_DNA.
DR Proteomes; UP000248783; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd00060; FHA; 1.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR032030; YscD_cytoplasmic_dom.
DR PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR Pfam; PF16697; Yop-YscD_cpl; 1.
DR SMART; SM00382; AAA; 3.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50901; FTSK; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell cycle {ECO:0000313|EMBL:PZR51569.1};
KW Cell division {ECO:0000313|EMBL:PZR51569.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248783};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 116..164
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 620..808
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 969..1159
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 638..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 986..993
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1457 AA; 152316 MW; 8373890CFE85F4AA CRC64;
MWRLSIEPTR DSGLAAVDVE VVAREGARVA DLARALGEHL AGSPETLLAP VTDGAPWPAG
LVLTQAPLRT GAVLPVMPVP ASWLGRAAPR RAARARVRVV AGPDAGLEVA VDTDACTVGR
GAGATVRLSD PAVSRLHARL LLVGGVVVQD EGSAHGTRVA GRPVVRAQPV AWGERVEVGR
TVLEVHRGDA PLAEPDAAVL RPPRFGEALE PAELEVPAPP AAPRRQPFPW PMMLMPALLG
GGMFLTSRSP FSLMFMIGFP LLMTVNHLVA RRQAAKEHDA ELRTWRADVE DVLARIDDAA
RVQRERAAQD EPDLVTVRER VAGGHPSTWV RTREDEDFLV VRAGTGPRPA VVTGQVARGG
DRVQRDLAVR EVEARRRLAG QPVPLVLAGQ RVVAVTSADR TRADAAVRAL LVRVAAAHSP
TDVVLAAVLG GAGEHVETWL RWLPHTAHRV AGAPPVAVGA TAGAALLDAL VGQDAARGRT
VCVVDEEAGV PRRVVEAVAA AGPERGVHLL WVGSDPDRVP SATDVLLDLD ALRVRRRDRG
GDDVLDTADT LDLAAAWHTA RALTACRDES AVVPPDSALP DAVRLPDLGT DLADPDDATA
VLDRWSAAAG LRAQLGAGPD GVVTVDLRED GPHGLVAGTT GSGKSELLQT LLCSLAVNNP
PSRITFLLVD YKGGAAFREC ADLPHTVGYI TDLTPALVQR ALVSLRAELA AREHLLAEHG
AKDLVALERL RPDVAPPSML ICVDEFAALL AEVPEFVDGV VDVAQRGRSL GMHLLLATQR
PAGVVTPQIK ANTDLRIALR MASTEDSGDV IDAPDAAALS RRTPGRAWLR RTGHGTRELV
QVAWVGAHEP VRDDAAAVQV RPFTVRAGAG PVPAAGQGRV HERSDLERLV LTVGEAFARS
GLPAPSRPWL PALEDEVQLA GGAPGTVLVG ARARDEAAVP GSAPDVHVCA PAPGTLPLGL
ADHPGTQDQR PLLVDYARAG HLLVHGASGS GKTELLRTVA AAATLAHDPA PAVVYGIDAA
GGGLGVLDAL PSVGSVVGEQ QPERVQRLVR MVHRTVVERN ALLARHGAAD IGALADAGVV
MPRVHLLVDN LPALVDQLES GGPLRRAHLD QLSAVLQDGR RCGVHVTATT PLRTGLPSAL
AASFGQRLVL RMTSVDDYQV LGVPQAVLDD ASPAGRGLLG RTEVQVATVG AAGTPEQGRA
LRELAARERD RYASQPPVAV PAMPTRVPAD LVPVPEADGV CVGVDADLAS GVVLSLLGGP
LLVTGRGGSG RTSFLLGLAD AAARSTVPPR RVRLLGPAAP AHPGVEPLDE PAAVLSALEE
HLAAPAPSGS AWDLVLVDDV HVWERGWERG GEDRRLVEEL ARLVEEGPAR RTAVVLATDA
DEARARQHVP GPVSVARRAR RAVLLGPEMA DGSLVGVTVP MHTHEPLGGV GRGLLVASGS
ARTVQVLSPS TERESVS
//