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Database: UniProt
Entry: I1D443_9PSEU
LinkDB: I1D443_9PSEU
Original site: I1D443_9PSEU 
ID   I1D443_9PSEU            Unreviewed;       844 AA.
AC   I1D443;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=DNA segregation ATPase, FtsK/SpoIIIE family {ECO:0000313|EMBL:EIE99717.1};
GN   ORFNames=SacglDRAFT_02832 {ECO:0000313|EMBL:EIE99717.1};
OS   Saccharomonospora glauca K62.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=928724 {ECO:0000313|EMBL:EIE99717.1, ECO:0000313|Proteomes:UP000005087};
RN   [1] {ECO:0000313|EMBL:EIE99717.1, ECO:0000313|Proteomes:UP000005087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K62 {ECO:0000313|EMBL:EIE99717.1,
RC   ECO:0000313|Proteomes:UP000005087};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Brambilla E., Klenk H.-P., Woyke T.J.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K62 {ECO:0000313|Proteomes:UP000005087};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA   Klenk H.-P., Woyke T.;
RT   "Noncontiguous Finished sequence of chromosome of Saccharomonospora glauca
RT   K62.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential cell division protein that coordinates cell
CC       division and chromosome segregation. The N-terminus is involved in
CC       assembly of the cell-division machinery. The C-terminus functions as a
CC       DNA motor that moves dsDNA in an ATP-dependent manner towards the dif
CC       recombination site, which is located within the replication terminus
CC       region. Required for activation of the Xer recombinase, allowing
CC       activation of chromosome unlinking by recombination.
CC       {ECO:0000256|ARBA:ARBA00024986}.
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; CM001484; EIE99717.1; -; Genomic_DNA.
DR   RefSeq; WP_005465406.1; NZ_CM001484.1.
DR   AlphaFoldDB; I1D443; -.
DR   STRING; 928724.SacglDRAFT_02832; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_2_2_11; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000005087; Chromosome.
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:0007049; P:cell cycle; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000005087};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        95..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          487..687
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          563..590
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         504..511
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   844 AA;  89784 MW;  11151CFE23634B12 CRC64;
     MASGSTTRGR GTARTGAGRG SQRSTKARTS SSKAKSGGRT TASRKPPAKR SKRSSGSALG
     RALRGAWTLL ARGVGGLARA VGRTRELDPE HRRDGLALGL IALALVAAVG VVWEGAGPVG
     EGIAVGTRSV IGSAAVALPV ALLMAAVVLM RSQPRPETRP RMVVGTVLIG LAVLGLLHLV
     SGRPQEHADQ MYAGGWIGWF SGDLLARGVT GWVAVPLLVL VLLYGVLVCA GTPIRRVPQR
     LREWTGAEAD ANADEEPPRR RTARSRTTEA DGADSGPEPD TETDSTTARP RGSTRKRKPA
     EPDEAQPTLD FAAPAESPTE ELARKPARAK AASKTARRRA PALSVTRTVE GDYKLPSLDL
     LTFGAESKGH SSANDAMIEA ITRVLEQFKI DAQVTGFTRG PTVTRYEVEL GPGVKVEKIT
     ALTKNIAYAV ATENVRLLAP IPGKSAVGIE VPNTDREMVH LGDVLRSPEA ASDDHPMVIG
     LGKDIEGNFV TANLTKMPHL LVAGSTGSGK SSFVNSMLVS LLARATPDEC RMILIDPKMV
     ELTPYEGVPH LITPIITQPK KAAAALAWLV EEMEQRYQDM QANRVRHIDD FNRKVRSGEI
     TAPPGSERVY RPYPYIMAIV DELADLMMTA PRDVEDAIVR ITQKARAAGI HLVLATQRPS
     VDVVTGLIKT NVPSRLAFAT SSLTDSRVIL DQPGAEKLIG MGDALYLPMG SGKPIRVQGA
     FVSDEEITAV VAATKEQAEP DYTEGVTTAK VGEKKDIDPD IGDDLDVLLQ AAELVVSSQF
     GSTSMLQRKL RVGFAKAGRL MDLLETRGVV GPSEGSKARE VLVKPEDLPG VLAMIRGDAP
     SAEE
//
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