ID Q7U329_HELHP Unreviewed; 941 AA.
AC Q7U329;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=DNA segregation ATPase FtsK/SpoIIIE {ECO:0000313|EMBL:AAP77050.1};
GN Name=ftsK {ECO:0000313|EMBL:AAP77050.1};
GN OrderedLocusNames=HH_0453 {ECO:0000313|EMBL:AAP77050.1};
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279 {ECO:0000313|EMBL:AAP77050.1, ECO:0000313|Proteomes:UP000002495};
RN [1] {ECO:0000313|EMBL:AAP77050.1, ECO:0000313|Proteomes:UP000002495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1 {ECO:0000313|Proteomes:UP000002495};
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; AE017125; AAP77050.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7U329; -.
DR STRING; 235279.HH_0453; -.
DR KEGG; hhe:HH_0453; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_4_1_7; -.
DR Proteomes; UP000002495; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000002495};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 606..796
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 171..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 857..888
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 175..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 623..630
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 941 AA; 106424 MW; 5F656A771C36BBDD CRC64;
MYPLFLFYPT YCLYKNTRLT FRRLELIVSF SLFFVALLIL QSLLFHKGSF GTSLLLFLKG
YIGYFGVWVL DLFFFLFSWL ISTKHNIDLL LKQMQNKILM GFDFFKHITT SSYIFTKKVL
THFITSITPS IQRLFAKNTQ DVLDLQTATQ EQTTRAHYDF KDVIVEETFD EMRPDSPSQT
ESAHTESTNM ATQPSLDTLE PIISPTPQTS QLQIVEASED TNLEDFFKNQ VAKHFDMLQN
LKLYQHTALS EPALKYSESK PTIPTQESTL PQESTPSQTD TLFQTSHTKE ISTPPPRPIN
PNVFLQTAPK QESITPIHIK NENIRAATQE STQSKQDSHT NTTLFDYAEY DDNLQTQMPQ
FTPFSLLTPM QSEVQPSIPT KQNTIPQHTQ NSIQPNTQDT ASHTMAQTLN INIQEIPTSN
IDWVDSIVQE IPQEQKPKPQ PSKIQVTEIA ENKALLDNLE YGKVNKPLHF KLPPISLLNQ
PFEEKNEIDE SEIDRKIEDL LAKLKMFRVE GDIVRTYSGP IVTTFEFRPA PHIKVSKILT
LEDDLAMALR ARSIRIQAPI PGKDVVGIEI PNNTMQTIYL REVLASDLFK TSTSPLTLAL
GKDIIGNPFI TDLKKAPHLL IAGTTGSGKS VGINAMILSL LYKNSPDNLK LLMIDPKKVE
FSIYADIPHL ITPIITQPKK AIVGLNSAVA EMDRRYDLMS EMRAKDIDSY NNKVLNEGGK
KFPYLVIIID ELADLMMTGG KEVEFSLARI AQMGRACGIH IIVATQRPSV DVVTGLIKTN
LPSRISYKVG SKIDSKVILD TFGAESLLGK GDMLFTPPRE GGVIRLHAPW NTEEEIEKVV
EFIKSQQNVE YDKNFMLDEK ENLMSENTEN LNNENNDLLT EAKNIILQDK KTSASYLQRR
LSIGYNKAAN IVEQLEREGF LSTPNVKGVR EILGDSSFKN D
//
