ID A0A1Q4WXH8_9PSEU Unreviewed; 811 AA.
AC A0A1Q4WXH8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:OKI14781.1};
GN ORFNames=A6A25_15115 {ECO:0000313|EMBL:OKI14781.1};
OS Saccharothrix sp. CB00851.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1835005 {ECO:0000313|EMBL:OKI14781.1, ECO:0000313|Proteomes:UP000186828};
RN [1] {ECO:0000313|EMBL:OKI14781.1, ECO:0000313|Proteomes:UP000186828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00851 {ECO:0000313|EMBL:OKI14781.1,
RC ECO:0000313|Proteomes:UP000186828};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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}.
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:OKI14781.1}.
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DR EMBL; LWLC01000065; OKI14781.1; -; Genomic_DNA.
DR RefSeq; WP_073899583.1; NZ_LWLC01000065.1.
DR AlphaFoldDB; A0A1Q4WXH8; -.
DR STRING; 1835005.A6A25_15115; -.
DR Proteomes; UP000186828; 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: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, ECO:0000313|EMBL:OKI14781.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000186828};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 78..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 450..650
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 467..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 811 AA; 86235 MW; CFD5489351990DD4 CRC64;
MAGRTGTSRK GTTRSSGAKP RAGASRPASK RSPAKRAAAK KSSSSIGKVW GLLGRGVGSV
VRAVGRGKEL DPAHRRDGLA LVLISLAVIT AAGVWWQAGG PVGQWVDVAV RSSVGGPAVI
VPVVLLAVGV TLMRTDPSPE ARPRLVIGSI LVAVGFLGMF HLVGGLPMDP IARRDAGGAL
GFLAGGFLAQ GLTPWVAGPL LVLIFAYGVL LLVHVPIREV PGKLGGLLHR KADQFDGFGA
EEVEPEPEEE KPAKLRRPSR SRRQAAATAE PDEQPELPLD EEPPPPPPAK STPKPKATPE
TSKAAAIAVR AVEGDYRLPP PTILKDGDAP KARSKANDVM IEAISGVLDQ FSIDAQVTGF
TRGPTVTRYE VELGPGVKVE KITALTKNIA YAVATDNVRL LAPIPGKSAV GIEVPNSDRE
MVRLGDVLRS PSTVKDNHPM VIGLGKDIEG HFVTANLTKM PHLLVAGSTG SGKSSFVNSM
LVSLLARATP DEVRMILIDP KMVELTPYEG IPHLITPIIT QPKKAAAALA WLVEEMEQRY
QDMQVNRVRH IDDFNRKVRS GEISAPPGSE RVYRPYPYIM AIVDELADLM MTAPRDVEDA
IVRITQKARA AGIHLVLATQ RPSVDVVTGL IKTNVPSRLA FATSSLTDSR VILDQPGAEK
LIGMGDGLYL PMGASKPVRI QGAYVADDEI SEIVNFTKDQ AQPEYTDGVT AAKAGEKKEI
DADIGDDLEL LIQAAELIVT SQFGSTSMLQ RKLRVGFAKA GRLMDLLETR GVVGPSEGSK
AREVLIKPDE LDSVVYLIRG GSGPGDDGDE D
//
