ID A0A2Z3JC30_9DEIO Unreviewed; 1017 AA.
AC A0A2Z3JC30;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:AWN22717.1};
GN ORFNames=DKM44_05285 {ECO:0000313|EMBL:AWN22717.1};
OS Deinococcus irradiatisoli.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2202254 {ECO:0000313|EMBL:AWN22717.1, ECO:0000313|Proteomes:UP000245368};
RN [1] {ECO:0000313|EMBL:AWN22717.1, ECO:0000313|Proteomes:UP000245368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17bor-2 {ECO:0000313|EMBL:AWN22717.1,
RC ECO:0000313|Proteomes:UP000245368};
RA Srinivasan S.;
RT "Complete Genome Sequence of Deinococcus sp. strain 17bor-2.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; CP029494; AWN22717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z3JC30; -.
DR KEGG; dez:DKM44_05285; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000245368; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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:AWN22717.1};
KW Cell division {ECO:0000313|EMBL:AWN22717.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000245368};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 673..864
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 485..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 691..698
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1017 AA; 110793 MW; F17B5B2F5B373B0F CRC64;
MTKAKKRART VQNRFDGEAL GLVLFALGIF LIITLVLPAQ GAGFMSQAHA ALMTWLSWGS
YTLPMVPLCY GILIFLNKEL RQLTRRLLGA AVVVLSLLAL QELFFPNTAG ALAALALGPL
RVVSYAAALL PIITLTLGIE LVLRLPALSL LKSFFRTLSA GVGLLLGWVQ AVIEARQEGK
ETAHQRQQVR QHLSAHSRDL ELLGKLYPDS RELQHWKDET KDAGRQVRAL DEHGLKDLEA
ELKHWRDVSS SFVLGAGRDL HAAVEREAPD AGAEIEMLAQ EVRAGRHELS LELPSTLASG
ALERLRRSLV MDLYRLSTKA GGLERERRRA AKALEKPDTT LLARERPAHA QRVQGWRELA
EAYAAWSERS APYAGWPELA RAYDASPTRL AETLEQALLT DPDAVLSERH VWEEKLEQAQ
PDSASAPLLD FDFGEAVSAA LGAGMTAQPP LIDLQLDGDR TAVSSELRPT ETLVMAAEPV
TVGVGSGAGQ APAPISPLPK PSGRNLDADS LPWEDEAEVT LPTPTRSRPQ QGALELALPG
VDLLDPIPPE VHNTAQLDLS ARQRAGLINE TLGQFGLAAK VVDFARGPTV TRYEIEPAPG
EKISRIASLS NDLARALAVG GVRVEAPVPG KSVIGLEVPN AEREPVTFHT AVAASTFKHT
RARLPIILGK SIDGELMVGD LAKMPHLLIA GSTGSGKSVC VNTLITSLLY KYLPTELRFL
MIDPKMVELT PYDGIPHLVR GVVTNPMDAA GVLLGAVAHM ERRYKMMSQI GAKNLEQYNA
KMRQVNETEL PHLVIIIDEL ADLMITSPKE VESAIMRLAQ MARATGMHLV LATQRPSVDI
LTSLIKVNVP ARIAFAVSSS HDSRTILDSM GAERLTGMGD MLFYQPGLIK PIRLQGPYIS
EDESNRITEE LRRQVFEDAF VELYGPDFDG AVESGGPSHD KANLDFSDPL LRQAAEICIE
EGQGSVSRLQ RRLSVGHARA GKLMDLLEAM GIVSKHQGSK PREVLINRED LPEYFGK
//