ID   A0A2U2ZYQ8_9ACTN        Unreviewed;      1527 AA.
AC   A0A2U2ZYQ8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:PWI17419.1};
GN   ORFNames=DI272_27100 {ECO:0000313|EMBL:PWI17419.1};
OS   Streptomyces sp. Act143.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2200760 {ECO:0000313|EMBL:PWI17419.1, ECO:0000313|Proteomes:UP000245455};
RN   [1] {ECO:0000313|EMBL:PWI17419.1, ECO:0000313|Proteomes:UP000245455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Act143 {ECO:0000313|EMBL:PWI17419.1,
RC   ECO:0000313|Proteomes:UP000245455};
RA   Valanrebinro G., Kumari S., Rameshkumar N.;
RT   "Actinomycin D producing novel Streptomyces isolated from the rhizosphere
RT   of saline tolerant kaipad rice and its draft genome analysis.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:PWI17419.1}.
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DR   EMBL; QFRX01000001; PWI17419.1; -; Genomic_DNA.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000245455; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR002543; FtsK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 2.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50901; FTSK; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Cell cycle {ECO:0000313|EMBL:PWI17419.1};
KW   Cell division {ECO:0000313|EMBL:PWI17419.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000245455}.
FT   DOMAIN          700..892
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1038..1232
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          226..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          302..329
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        230..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         718..725
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1055..1062
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1527 AA;  164539 MW;  4AA9ECCCD630E380 CRC64;
     MRLTLTVVDP FGGGTADVVL DADPESTVGD IAQELAKQVG AAGGAQVIPL GLQQHQIPAH
     NAPLLYVDGY GVDPSATVVN SPLRDGAVVS LQDPAGCLPG EPTGLVELRV VGGPVAGFVH
     RLGVGRYDIG SGPASYIRID DPELDARALT LSVATDGTCQ VTVHTKAESD DDPAPVTLDG
     TAVEEDKTDW PLGGQIAVGN TLLELTRYSP PNAALKWSDD GIGLDYNRPP RLRPPDRQTK
     FRLPSPPREY EARPLPWLMA LTPLVGAIVS VLIFQRWYYL IMAGLSPILL FANYFNDKKH
     GRKSHAKQVK EYEEQKEKVE KDAQDALVAE RTDRRHAIPD PATVLSLGTG PRTRLWERRR
     TDRDHLLIRV GTGQLDSEVV LDDPEQLDHK RQVTWKIEDA PVALSLRSLG VIGMAGPGDS
     ARAMGRWAVA QTAALHSPMD VQFYVLSENS AQESWDWTRW LPHARPGSGQ DVNVLIGTDA
     ETVGARIGEL TQILDARKKA AEQNKGQGTG FSDPDIVVVW DGSRRLRSLP GVVRILREGP
     AVSLYALCLD AEERFLPGEC QAYVVAEPPA QEYDYLQQAQ SQQPVAGGGF PSFQAWHHTG
     QDSSHTEAAA DKLRLRVEEA GAERIKDVRP DFVSPTWCLR LARALSPLRD ISGETEDSAL
     PAASRLLDVL QLEPPTSDAI VARWRMGGQS TLAVIGESYD GPFGIDIRKD GPHGLIAGTT
     GSGKSELLQT IVAALAVANT PENMTFVLVD YKGGAAFKDC VHLPHTVGMV TDLDAHLVER
     ALESLGAELH RREHILAAAD AKDIEDYQDL VRRDPSHAPV PRLLIVIDEF ASMVRDLPDF
     VTGLVNIAQR GRSLGIHLLL ATQRPSGVVS PEIRANTNLR IALRVTDGGE SSDVIDSPEA
     GHISKSTPGR AYVRLGHASL VPFQSGRVGG RRPGAADPAV LMPWVGPLSW EDLGRAALVK
     PKAESREDEE ITDLKVLVDT IRDANSSLGI PPQHSPWLPA LDETLLLDDI QVPAFAGGPG
     KLPPAPYGVE DLPAQQARRP VAVDFASFGH LMIGGAPRSG RSQVLRTLAG SIARTHSVAD
     VHMYGIDCGN GALNALTRLP HVGAVVGRNQ TERVVRLVNR LKGEMDRRQN LLADKGFADI
     GEQRASVAED ERLPHIVVLL DRWEGWVPTL GEVDHGSLTD ELQTMMREGA SVGIHLVLTG
     DRTLLVGRIA TLTEDKYGLR LADRSDFSAL GIPARKVPEE IPPGRGFRNE FGTETQFALL
     SEDTTGQGQA AALAAIGEAA AARDAAVPRS HRPFRVDSLP SRVSFPEAWE MRDPEASRAK
     LWGLVGIGGD EIVGFGPDLS QGVPTFVVAG PAKSGRSTVL MNFAQSYLTQ GVRLVIAAPR
     QSPLRQLDGT EGVLKVFTGD DIDEDEFEEL MDEASLEEPI VVLVDDGEIL EDCDAESQLK
     KLVSRGAERG LAMVIAGDEE DVCSGFSGWQ VDAKKARRGI LLSPQETSSG DLIGVRLNRG
     LVGGQITPGK GMLHLGDGEL RTVVVPG
//