ID A0A240BQY5_SERFI Unreviewed; 1194 AA.
AC A0A240BQY5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN Name=ftsK {ECO:0000313|EMBL:SNV98331.1};
GN ORFNames=SAMEA4384070_01735 {ECO:0000313|EMBL:SNV98331.1};
OS Serratia ficaria.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=61651 {ECO:0000313|EMBL:SNV98331.1, ECO:0000313|Proteomes:UP000215134};
RN [1] {ECO:0000313|EMBL:SNV98331.1, ECO:0000313|Proteomes:UP000215134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12148 {ECO:0000313|EMBL:SNV98331.1,
RC ECO:0000313|Proteomes:UP000215134};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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}.
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DR EMBL; LT906479; SNV98331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A240BQY5; -.
DR STRING; 1411141.GCA_001590885_03018; -.
DR KEGG; sfj:SAMEA4384070_1735; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000215134; Chromosome 1.
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:0007059; P:chromosome segregation; 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; 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 Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
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}; Reference proteome {ECO:0000313|Proteomes:UP000215134};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 22..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 837..1050
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 344..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..674
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 854..861
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1194 AA; 128902 MW; E31F2837A81D82F4 CRC64;
MSQEYTEDKE VTLRKLSSGR RLLEAVLIVV AIFAVYLMAA LVSFNPSDPS WSQTAWHEPI
HNLGGGVGAW MADTLFFTFG VLAYAIPPIM LVLCWAAYRQ RGSGEYIDYF ALSLRLIGTL
ALVLTSCGLA ALNVDDLYYF ASGGVIGSLL SNAMLPWFNG IGATLALLCV WAAGLTLFTG
WSWLVIAEKI GGAVLGVATF MTNRSRREDR YHDDERYLDD EPGLAEKGAT AVAATAATAA
AADDDVLFSA PSVAETAKSA AEDAEDPLLS GLRASDDDDI DAAAATPAPA PAPVNEAVTA
APVVAQAPSV TVAPAAPAKV SQHPMSAPAE NAAPPLYSFE IPEETPAPKV TRPVDPYQDD
DEPRLGNWQA PAAPQPRDHS PFDFSAAQSD QVDVSGSSGF DAADAAATPF GNARPQLDTA
AAAAAAGAAA TTFMPAFTAT SDGNPQVKQG IGPELPRPNP VRIPTRRELA SYGIKLPSQR
AAEQDQRQVE AEPQPPIGAN PQDEEAMQEA ALRQAFAEQQ NQRYGEDYQQ DDEEALQEAA
LRQAFAEQQQ ARYGQQPEPE PRVQTPAASS VDTRNAFSFS PMDDLVDDGP GEPLFTLSPQ
LEERIEQQSE REDDVPFGQF EPAAPAYQPP QPQTPPAQQA YQQPAQPQQQ PYQQPQQPAQ
PPSYQQPAAQ PAPAAPQQPA MDSLIHPFLM RNDQPLQKPT TPLPTLDLLT EAPKEVEPVD
TFALEQKARL VEASLADYRV KADVVDILPG PVITRFELDL APGVKAARIS NLSRDLARSL
STSAVRVVEV IPGKPYVGLE LPNVKRQTVY LREVLDCPAF RDNPSPLSIV LGKDISGEPV
VADLGKMPHL LVAGTTGSGK SVGVNAMILS ILYKATPKEV RFIMIDPKML ELSVYEGIPH
LLTDVVTDMK DAANALRWCV GEMERRYKLM SALGVRNLAG YNERVDQAEA MGRPIPDPFW
KPTDSMDITP PVLEKEPYIV VMVDEFADLI MTVGKKVEEL IARLAQKARA AGIHLVLATQ
RPSVDVITGL IKANIPTRIA FTVSSKIDSR TILDQGGAES LLGMGDMLYL APNSSIPVRV
HGAFVRDQEV HAVVKDWKAR ERPQYKEGIL SGGEDGEGGA GGGMEGDEEL DPLFDQAVEF
VVDKRRASIS GVQRQFRIGY NRAARIIEQM EAQGIVSEQG HNGNREVLAP PRHD
//