ID I2ND51_9PAST Unreviewed; 1000 AA.
AC I2ND51;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=HMPREF1054_0599 {ECO:0000313|EMBL:EIG23762.1};
OS Haemophilus paraphrohaemolyticus HK411.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1095743 {ECO:0000313|EMBL:EIG23762.1, ECO:0000313|Proteomes:UP000003345};
RN [1] {ECO:0000313|EMBL:EIG23762.1, ECO:0000313|Proteomes:UP000003345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK411 {ECO:0000313|EMBL:EIG23762.1,
RC ECO:0000313|Proteomes:UP000003345};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (APR-2012) 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:EIG23762.1}.
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DR EMBL; AJMU01000074; EIG23762.1; -; Genomic_DNA.
DR AlphaFoldDB; I2ND51; -.
DR PATRIC; fig|1095743.3.peg.1744; -.
DR eggNOG; COG1674; Bacteria.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000003345; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; 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};
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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 652..865
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 194..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 669..676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1000 AA; 110447 MW; DE6BE1F998862227 CRC64;
MIRRLKGKET AFNFLFALCG LFGIYLILAW ASYSPLDNAW SVASTATSEP LNKTGMFGAW
MIDLLYAFFG KVAFLLPFSL TGFSAYMLLT RGAENATFKG ILLRSLSFFV LMIGLAGLAN
TILSNSPNYL SGGFVGAMSQ GLMSEHIGQF GSLFVAMLLT AIGFYFCSGQ TLIPLLMNFY
DWVSAKDTKV EEKPLQVRPV AEVEPTEDDL QVDSENSPLT SETQLEGQSE ERAEAVISMD
EQLTDLTLFK RPNISGLQQA SPAEIYSAET SSSEIASDIK PTTVAKTAEM NLFNPADMHT
ELPKIRLPEL ETEVQPTQTE NNIGLNVELP KVRLNPVEPQ AEPMEQAVDF TENSANQHTQ
PKISVRLTNE DSGVDAIEQA ASENEVLHFM QSPSPVIKLR AEDEEREEQE EDFDAIRERE
FAEMERKRLA EIEARAKAAG LEHTFNKITE GSSHFETDLP TNVQIRTEPT PSKFTTPLKA
AVGAEGHLPP DYPRGGYGET LIHPLLQGSK KLEKPTTPLP TLDLLEEHHP SGQQMTEGEI
IATSRRIETA LANYGVKATV EDVLVGPVVT RYEIKPAVGV KAAKITSLAS DLAREMMSTI
RITDVVPGKP YMGIEVPNPH REIVWLRDLI ASDEFRYTKA KLPMILGKDL ANKPVIMDMV
ETPHLLVAGQ TGGGKSVGIN TMILSLLYKL TPEQVRLIMI DPKQVELSVY NDIPHLLTPV
VIDMKKAANA LRWAVDEMER RYTLLTHLNV RNITGYNNKI DEAEAMGMPI ADPSWKEGDS
MDKMPPALGK LSYIVLVVDE FADLMMTAGK EVEEYIMRIS QKARAVGIHL ILATQRPSTD
VITGVIKANI PSRIAFTVAS PYDSRTILDS IGAENLLGRG DMLYSKAGSP ELVRVHGAYM
SDDDVMNVAD NWKARGKPEY IESILESLQE PEERSEGGTG ELDARFDEVV AFVLETGITT
ASGIQRKLNL GFPRAARILD QMEQEGILSA PDHRGRREII
//
