ID L7EXW4_9ACTN Unreviewed; 1538 AA.
AC L7EXW4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN ORFNames=STRTUCAR8_04631 {ECO:0000313|EMBL:ELP64253.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP64253.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP64253.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP64253.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:ELP64253.1}.
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DR EMBL; AEJB01000465; ELP64253.1; -; Genomic_DNA.
DR RefSeq; WP_006380726.1; NZ_AEJB01000465.1.
DR STRING; 85558.T45_07318; -.
DR PATRIC; fig|698760.3.peg.6896; -.
DR Proteomes; UP000010931; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 CDD; cd00060; FHA; 1.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 2.60.200.20; -; 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 InterPro; IPR008984; SMAD_FHA_dom_sf.
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 SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50901; FTSK; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000010931};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 257..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 710..902
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1049..1243
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 228..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 304..331
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 232..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 728..735
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1066..1073
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1538 AA; 165773 MW; A4A70C3E0FEDE58F CRC64;
MRLTLTVVDP FGGSTADVVL DADPESTVGD IAQELAKQVG HSGAQIIPIG QHGQHAQHGQ
HGRVPPNNAP LVYVDGYAVD PSANVLGSPL REGAVVSLQD PAGCLPGEPT GLVELRVVGG
PVAGFVHRLG VGRYDIGSGP ASYIRIDDPE VDARALTLSV ATDGTCQVTV HGEKDGVTLD
GEEIADVKGT EWPLGGQIAV GNSLVELARY TPPNAALKWS EDGVGLDYNR PPRLRSPDRQ
TKFRLPSPPR DFEARPLPWL MALTPLVGAI VAVTIFGRWY YLIMAGLSPI LLFANYFMDK
KHGRKSHAKQ VKEYKEQKER IEKDAQDALL AERQDRRHAI PDPATVLSLG TGPRTRLWER
RRTDRDHLLL RVGTGQLPSE VVLDDPEQDE HRRQVTWKIE DAPVALSLRS LGVIGMAGPG
DSARALGRWA VAQTAALQSP MDVQFYVLSE STAQDSWDWV RWLPHTRPSG GQDVNVLIGT
DAETVGARIG ELTQILDARK KAAEQNKGQR ASFSDPDIVV VWDGSRRLRS LPGVVKLLRE
GPAVAMYALC LDAEERFLPG ECQAFVVAEP RAEEHTDPAY AAGLGTSAPS QPQVAGGFPA
FPSFHAWHAA DSEPDRRAQA DKLRLRVEEE SAERVRDVRP DFVSAAWCLR LARSLSALRD
ISGETEDSAL PGSSRLLDVL QLEPPTPDAI TARWRMGGQS TMAVIGESYD GAFGIDIRKD
GPHGLIAGTT GSGKSELLQT IVAALAVANT PENMTFVLVD YKGGAAFKDC VHLPHTVGMV
TDLDAHLVER ALESLGAELH RREHILANAD AKDIEDYQDL VRRDPSHPPV PRLLIVIDEF
ASMVRDLPDF VTGLVNIAQR GRSLGIHLLL ATQRPSGVVS PEIRANTNLR IALRVTDGGE
SSDVIDSPEA GHISKNTPGR AYVRLGHASL VPFQSGRVGG RRPGAADPAV LMPWSGALAW
EDLGRAALKK PKVEKREDEE ITDLKVLVDA VRDANRSLGI PPQHSPWLPA LSETLLLDEI
EVPAFADHGT GRLAPVPYGV EDLPSAQARR PVVVDFSTFG HLMIGGAPRS GRSQILRTIA
ASLARTHSTA DVHLYGIDCG NGALNALTRL PHCGAVVSRN QTERVIRLVN RLKAEMSRRQ
DLLAEKGFAD IGEQRAASPA EERLAHIVVL LDRWEGWVPT LGEVDHGTLT DELTTMMREG
ASVGVHLVLT GDRTLLVGRI ATLTEDKYGL RLADRSDFSA LGIPHRKVPE EIPPGRGYKN
ESGIETQFAL LSEDTTGQGQ AAAITAIGEA ATARDAQVPR SRRPFRVDSL PSRINFADAW
GMRDPETSGS RLWGLVGIGG DDITGFGPDL ATGVPTFVIA GPAKSGRSTV LMNFAQSYLS
QGVRLVIAAP RQSPLRQLDG ADGVLKVYTG DDIDEDDFEE IIDKASLEEP IVVLIDDGEI
LEDCDAASQM KKIVSRGAER GLGLVIAGDE EDVCSGFSGW QVDAKKGRRG ILLSPQESSS
GELIGVRINR GMVGGQIAPG KGMLHLGDGE LRTVVIPG
//
