ID L8PHK4_STRVR Unreviewed; 938 AA.
AC L8PHK4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Putative FtsK/SpoIIIE family protein {ECO:0000313|EMBL:ELS57046.1};
GN ORFNames=STVIR_2060 {ECO:0000313|EMBL:ELS57046.1};
OS Streptomyces viridochromogenes Tue57.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160705 {ECO:0000313|EMBL:ELS57046.1, ECO:0000313|Proteomes:UP000011205};
RN [1] {ECO:0000313|EMBL:ELS57046.1, ECO:0000313|Proteomes:UP000011205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tue57 {ECO:0000313|EMBL:ELS57046.1,
RC ECO:0000313|Proteomes:UP000011205};
RX PubMed=23788550;
RA Gruning B.A., Erxleben A., Hahnlein A., Gunther S.;
RT "Draft Genome Sequence of Streptomyces viridochromogenes Strain Tu57,
RT Producer of Avilamycin.";
RL Genome Announc. 1:E00384-13(2013).
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 -!- 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:ELS57046.1}.
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DR EMBL; AMLP01000065; ELS57046.1; -; Genomic_DNA.
DR AlphaFoldDB; L8PHK4; -.
DR PATRIC; fig|1160705.3.peg.2050; -.
DR Proteomes; UP000011205; Unassembled WGS sequence.
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 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}; 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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 115..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 587..787
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 604..611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 938 AA; 99787 MW; E001515A3F4795DC CRC64;
MKQWAHVSTA FSTGNLTSMA SRPSAAKKPP AKKAAASAKA PAKKAAAKKA PAKKAPAKKA
AAKKAAPPKP APSPTGGIYR LVRAVWLGLA HAVGAVFRGI GQGAKNLDPA HRKDGVGLLL
LGLALIVAAG TWSNLRGPVG DLVEMLVTGA FGRLDLLVPI LLSVVAVRFI RHPEKPEANG
RIVIGLSALL IGVLGQVHIA VGSPARSEGM QAIRDAGGLI GWGAATPLTY TMGDVLAVPL
LVLLTIFGLL VVTATPVNAI PQRLRQLGVR LGILPDPTER DELTDDDQRY DDQWREALPA
SRSRRRGPAP EAYDPDSAEQ EALSRRRGRP RRSAVPQPEM NRPMDAVDVA AAAAAALDGA
VLHGMPPSPI VADLTQGVSV GDRAETTPVP TPVPAARPKQ EKLPKTEVPD LTKPAAPDLT
KSEVPDLTKS APDEIRDLPP RAEQLQLSGD ITYSLPSLDL LERGGPGKTR SAANDAIVES
LTTVFTEFKV DARVTGFTRG PTVTRYEVEL GPAVKVERIT ALTKNIAYAV ASPDVRIISP
IPGKSAVGIE IPNTDREMVN LGDVLRLAAA AEDDHPMLVA LGKDVEGGYV MANIAKMPHV
LVAGATGSGK SSCINCLITS VMMRATPEDV RMVLVDPKRV ELTAYEGIPH LITPIITNPK
RAAEALQWVV REMDLRYDDL AAYGYRHIDD FNEAVRNGKV KAPEGSEREL QPYPYLLVIV
DELADLMMVA PRDVEDAIVR ITQLARAAGI HLVLATQRPS VDVVTGLIKA NVPSRLAFAT
SSLADSRVIL DQPGAEKLIG KGDGLFLPMG ANKPVRMQGA FVTEDEVAAV VQHCKDQMAP
VFRDDVVVGT KQKKEIDEDI GDDLDLLCQA AELVVSTQFG STSMLQRKLR VGFAKAGRLM
DLMESRGIVG PSEGSKARDV LVKPDELDGV LAVIRGEA
//
