ID C5ZVU0_9HELI Unreviewed; 1125 AA.
AC C5ZVU0;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN ORFNames=HCAN_0303 {ECO:0000313|EMBL:EES89021.1};
OS Helicobacter canadensis MIT 98-5491.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537970 {ECO:0000313|EMBL:EES89021.1, ECO:0000313|Proteomes:UP000007032};
RN [1] {ECO:0000313|EMBL:EES89021.1, ECO:0000313|Proteomes:UP000007032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX PubMed=19542273; DOI=10.1128/JB.00729-09;
RA Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA Weinstock G.M., Wren B.W., Pallen M.J.;
RT "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL J. Bacteriol. 191:5566-5567(2009).
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; CM000776; EES89021.1; -; Genomic_DNA.
DR AlphaFoldDB; C5ZVU0; -.
DR STRING; 537970.HCAN_0303; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_6_7; -.
DR Proteomes; UP000007032; Chromosome.
DR GO; GO:0016020; C: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 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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000007032};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 801..991
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 185..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 818..825
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1125 AA; 126636 MW; A371A62DD6A75DBE CRC64;
MLGILSIVGE FGLLGAIGKA YAHLHFNLFG YFGYIWLLIL AYLFYKNTAD TKERIIEKTL
GIVIIGLALL ILQGLFISDA GFFSNAFSSI LKSFINPLGI FGLTLILILL GIMLYTGKSA
KTLLHSFIKG LKDDLQKTPK EESKQSKKES FFLRLKAFFT PPNKISQRRN PHSLTLEELA
SLSKNAPSTP NIIQETQETK RESELDDLSS TKPTEEKSLE ETPNPLEIKE IESSSLPYPT
DIPKIENELQ YTPNSTANEE SKIRLIPTQE AQGPKNHNLK QFQMESIMSL ERFKNFEKSI
FLQEEKEEKD EPIKLIKKDQ TENSTSQSTQ DTYKFPIPQE SQNLQEPNPE VLSSKEDLSP
KESPKPIKAY PKKLYSATPF SAYYDKDPTD ATRNCLVPNN PESSQNQAPA VNEVEAITKN
EAQQASEDED IKAIQTAIKE ELQKAQDFLH YQTQESSPQF VEVENEIVQQ ETQAAIEEKS
EDKKDITPNL DHLAKTNPQT TFEESSLQES PINPIPQEAP LLKNINFPVY GYGNTFNQAP
QEINPNSTLQ ELPQQKSQEN APTPITPQSQ QETLEILQNA IREKRDLTLQ FKEEITLTPT
KIPLESNQNQ QNQSTPNAQE SITQTTPQTP QPQTNTTQVK ILEENQNLLK EIETNTELKP
IQTDFILPKL DFLQTPQEER IEIDEDEIDK KINDLLNKLR MFKIEGDIVR TYSGPIVTTF
EFRPSPNVKV SRIQTLQDDL AMALRAKTIR IQAPVPGKDV VGIEIPNSQI QTIYLREILE
NEIFQNAASP LTLALGKDIV GNPFVTDLKK LPHLLIAGTT GSGKSVGINA MILSLLYKNS
PDTLRLLMID PKMLEFSIYN DIPHLLTPVI TQPKKAIIAL DNAVKEMERR YTLMSEARIK
NIESYNKKAE IEGFEPFPYI VIVIDELADL MMSGGKEAEL SIARLAQMAR ASGIHLIVAT
QRPSVDVVTG TIKANLPSRI SYKVGQKIDS KVILDSFGAE SLLGRGDMLF TPPGGGIVRL
HAPWSTEEEI EKIVEFIKSQ RPVQYNENFM PNEDETLGLN YEGETDELYE EAKRIMLADN
KTSISYIQRR LGIGYNKAAN IVEQMTARGF LSQPNSKGAR EIIGE
//
