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Database: UniProt
Entry: I9SDC6_HELPX
LinkDB: I9SDC6_HELPX
Original site: I9SDC6_HELPX 
ID   I9SDC6_HELPX            Unreviewed;       845 AA.
AC   I9SDC6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:EJB54674.1};
GN   Name=ftsK {ECO:0000313|EMBL:EJB54674.1};
GN   ORFNames=HPHPH28_1130 {ECO:0000313|EMBL:EJB54674.1};
OS   Helicobacter pylori Hp H-28.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=992041 {ECO:0000313|EMBL:EJB54674.1, ECO:0000313|Proteomes:UP000005158};
RN   [1] {ECO:0000313|EMBL:EJB54674.1, ECO:0000313|Proteomes:UP000005158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hp H-28 {ECO:0000313|EMBL:EJB54674.1,
RC   ECO:0000313|Proteomes:UP000005158};
RA   Blanchard T.G., Czinn S.J., McCracken C., Abolude K., Maroo A.,
RA   Santana-Cruz I., Tallon L.J., Ficke F.W.F.;
RT   "Genome sequence of Helicobacter pylori Hp H-28.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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:EJB54674.1}.
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DR   EMBL; AKOI01000011; EJB54674.1; -; Genomic_DNA.
DR   RefSeq; WP_000837219.1; NZ_AKOI01000011.1.
DR   AlphaFoldDB; I9SDC6; -.
DR   PATRIC; fig|992041.3.peg.1098; -.
DR   Proteomes; UP000005158; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR   CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
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; IPR003593; AAA+_ATPase.
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; PF17854; FtsK_alpha; 1.
DR   Pfam; PF09397; FtsK_gamma; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 1.
DR   SMART; SM00382; AAA; 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}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          519..709
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          175..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         536..543
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   845 AA;  94711 MW;  E3DBCE05AED1B1FA CRC64;
     MKSKKLYLAL IIGVLLAFLT LSSWLGNSGL VGRFGVWFAA INKKYFGYLS LINLPYLAWV
     LFLLYKAKNP FTEIVLEKTL GHLLGILSLL FLQSSLLNQG EIGNSARLFL RPFIGDFGLY
     ALIMLMVVIS YLILFKLPPK SVFYPYINKT QNLLKEIYKQ CLQAFSPNFS LKKEGFENTS
     SDTQKKETKN EKEKENLKEN PIDENHKTPN EESFLAIPTP YNTTLNDLKP QEGLVQISSH
     PPTHYTIYPK KNRFDDLSNP TNPTLKETKQ ETKEREPTPT KETLTPTTPK PIMSAPAPNT
     ENDNKTQNHK APNHPIKEEN AQENAQEEMI EENLKEEEAQ DAPSFSPVIP TSTKKPVMVK
     ELSENKEILD GLDYGEVQKP KDYELPTTQL LNAVCLKDTS LDENEIDQKI QDLLSKLRTF
     KIDGDIIRTY SGPIVTTFEF RPAPNVKVSR ILGLSDDLAM TLCAESIRIQ APIRGKDVVG
     IEIPNSQSQV IYLREILESE LFQKSSSPLT LALGKDIVGN PFITDLKKLP HLLIAGTTGS
     GKSVGVNAMI LSLLYKNPPD QLKLVMIDPK MVEFSIYADI PHLLTPIITD PKKAIGALQS
     VAKEMERRYS LMSEYKVKTI DSYNEQAENN GVEAFPYLIV VIDELADLMM TGGKEAEFPI
     ARIAQMGRAS GLHLIVATQR PSVDVVTGLI KTNLPSRVSF RVGTKIDSKV ILDTDGAQSL
     LGRGDMLFTP PGTNGLVRLH APFATEDEIK KIVDFIKAQK EVQYDKDFLL EESRMPLDTP
     NYQGDDILER AKAVILEKKI TSTSFLQRQL KIGYNQAATI TDELEAQGFL SPRNAKGNRE
     ILQNF
//
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