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Database: UniProt
Entry: B5ZAC6_HELPG
LinkDB: B5ZAC6_HELPG
Original site: B5ZAC6_HELPG 
ID   B5ZAC6_HELPG            Unreviewed;       859 AA.
AC   B5ZAC6;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Cell division protein {ECO:0000313|EMBL:ACI27106.1};
GN   Name=ftsK {ECO:0000313|EMBL:ACI27106.1};
GN   OrderedLocusNames=HPG27_340 {ECO:0000313|EMBL:ACI27106.1};
OS   Helicobacter pylori (strain G27).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=563041 {ECO:0000313|EMBL:ACI27106.1, ECO:0000313|Proteomes:UP000001735};
RN   [1] {ECO:0000313|EMBL:ACI27106.1, ECO:0000313|Proteomes:UP000001735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G27 {ECO:0000313|EMBL:ACI27106.1,
RC   ECO:0000313|Proteomes:UP000001735};
RX   PubMed=18952803; DOI=10.1128/JB.01416-08;
RA   Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA   Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT   "The complete genome sequence of Helicobacter pylori strain G27.";
RL   J. Bacteriol. 191:447-448(2009).
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
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DR   EMBL; CP001173; ACI27106.1; -; Genomic_DNA.
DR   RefSeq; WP_000837277.1; NC_011333.1.
DR   AlphaFoldDB; B5ZAC6; -.
DR   KEGG; hpg:HPG27_340; -.
DR   HOGENOM; CLU_001981_4_0_7; -.
DR   Proteomes; UP000001735; 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   GO; GO:0051301; P:cell division; 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}; Cell cycle {ECO:0000313|EMBL:ACI27106.1};
KW   Cell division {ECO:0000313|EMBL:ACI27106.1};
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}; 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          533..723
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          172..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..371
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        309..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         550..557
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   859 AA;  96580 MW;  59E9410A99B6C133 CRC64;
     MKSKKLYLAL IIGVLLAFLT LSSWLGNSGL VGRFGVWFAA LNKKYFGYLS FINLPYLAWV
     LFLLYKTKNP FTEIVLEKTL GHLLGILSLL FLQSSLLNQG EIGNSVRLFL RPFIGGFGLY
     ALIMLMVVIS YLILFKLPPK SVFYPYINKT QSLLKEIYKQ CLQAFSPNFS PKKEGFENTP
     PDIQKKETNN DKEKENLKEN PIDENHKTPN EESFLAIPTP YNTTLNDLKP QEGLVQISSH
     PPTHYTIYPK RNRFDDLTNP TLKKTQQETK EREPTLTKET LTPTTPKPAT LKPIMPISAP
     NTENHDKTQN PKTPNHPIKE DDLQESPQEN PQKENQKENI EEKENLKEEE KEIQNAPSFS
     PLTPTSAKKP VMVKELSENK EILDELDYGE VQKPKDYELP TTQLLNTVCL KDTSLDENEI
     DQKIQDLLSK LRTFKIDGDI IRTYSGPIVT TFEFRPAPNV KVSRILGLSD DLAMTLCAES
     IRIQAPIKGK DVVGIEIPNS QSQIIYLREI LESELFQKSS SPLTLALGKD IVGNPFITDL
     KKLPHLLIAG TTGSGKSVGV NAMILSLLYK NPPDQLKLVM IDPKMVEFSI YADIPHLLTP
     IITDPKKAIG ALQSVAKEME RRYSLMSEYK VKTIDSYNEQ APNNGVEAFP YLIVVIDELA
     DLMMTGGKEA EFPIARIAQM GRASGLHLIV ATQRPSVDVV TGLIKTNLPS RVSFRVGTKI
     DSKVILDTDG AQSLLGRGDM LFTPPGTNGL VRLHAPFATE DEIKKIVDFI KAQKEVEYDK
     DFLLEESRMP LDTPNYQGDD ILERAKAVIL EKKITSTSFL QRQLKIGYNQ AATITDELEA
     QGFLSPRNAK GNREILQNF
//
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