ID A0A1Q4FDX7_9SPHI Unreviewed; 834 AA.
AC A0A1Q4FDX7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:OJY91769.1};
GN ORFNames=BGP14_22745 {ECO:0000313|EMBL:OJY91769.1};
OS Sphingobacteriales bacterium 44-15.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895837 {ECO:0000313|EMBL:OJY91769.1, ECO:0000313|Proteomes:UP000186250};
RN [1] {ECO:0000313|EMBL:OJY91769.1, ECO:0000313|Proteomes:UP000186250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44-15 {ECO:0000313|EMBL:OJY91769.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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}.
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:OJY91769.1}.
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DR EMBL; MKWG01000003; OJY91769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4FDX7; -.
DR STRING; 1895837.BGP14_22745; -.
DR Proteomes; UP000186250; 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, ECO:0000313|EMBL:OJY91769.1};
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 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 482..686
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 257..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 499..506
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 834 AA; 93071 MW; 7AB1FAF5FB893E2B CRC64;
MANKLKSNKS KKADPEKLTA DKEEKVKVKE LVKDERTHKI IGSILLLSAF FLFVAFTSYL
FTWRQDQDKV FQGFSSFLFG DNIKSANLLG KIGAYISHIF FYKGFGLSSY LFCSFFFILG
VNLLFGRKIF SPWRNFRYIV VGLIFFSTAF AFMARRSGFP WGGEIGNISS DWLSSLIGNV
GTAALLLAGG FSYFIWRFNP VFTIPAYKSS KKGSEKEKFV PVDNSFSEEA RLFADPDILE
EKTNKVKHGG GVVVIPPANE ANSEKGVSGN TASLSVPPDP EQIKKGKTNL TGKKNRTEEL
ELQIQPHYED TEEAEEEQLP EEEEAPAVAH VENLPPYDPV LDLRDYEYPS LELLETHGSE
KIVLDSAELE ANKNQIINTL KNYDIDIRQI YATVGPTVTL YEIVPAAGVR ISRIKNLEDD
IALSLAALGI RIIAPIPGKG TIGIEVPNVK KAIVSMKGLL STDKFQQNKF SLPIALGKKI
DNEHFIVDLA TMPHLLMAGA TGQGKSVGIN AILVSLLYKK HPSQLKLVMV DPKKVELSLY
RVIEKHFLAK LPGEEESIIT DTKKVVHTLN ALCIEMDNRY DLLKEAGCRN IREYNEKFVA
RKLNPEKGHQ FLPFIVLVID EFADLIMTAG KEIEMPIARL AQLARAVGIH LIIATQRPSV
NIITGTIKAN FPARVAFKVS SKIDSRTILD AGGAEQLIGR GDMLVSYNGE ITRVQCAFVD
TPEVEKIVEF ISDQRGYPQP FYLPEYVDEK ELESRDFDSG NRDPLFEEAA RMIVQSQVGS
TSLLQRRMKL GYNRAGRLMD QLEAAGIVGA NQGSKARDVL FKTEMELEEF LQAL
//
