ID A0A0Q5LBP0_9MICO Unreviewed; 1397 AA.
AC A0A0Q5LBP0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN ORFNames=ASF82_11860 {ECO:0000313|EMBL:KQR44812.1};
OS Frigoribacterium sp. Leaf164.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR44812.1, ECO:0000313|Proteomes:UP000051005};
RN [1] {ECO:0000313|EMBL:KQR44812.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR44812.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR44812.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR44812.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQR44812.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMOX01000003; KQR44812.1; -; Genomic_DNA.
DR STRING; 1736282.ASF82_11860; -.
DR Proteomes; UP000051005; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000051005};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 569..763
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 909..1103
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1102..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 587..594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 926..933
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1397 AA; 146357 MW; 6686241C00E4AFC0 CRC64;
MLEGSVLTIG GPPGVAALPP DLPSIRIVGG PGAGTVFHVD PGTVVVGSAP EATVRLAARG
VAPVAALVQL DGASRFSITP VACDDADVPP VTVDGVPLTT TVALTPSSVV ELGEVLLGVA
DAGTASAAIG LAEGGGRLEH ARPPRLLPEP PTTAFRYPAQ PQAPPRRPLP IVAAAAPLLM
GGVMVLVLDN PTFLVFGLLS PVILIGNYLY DRRNGRVTHR DALASHAATR QAVAADAAEA
VVRRQDELRS SCPDAATLLD LAVRRRARLW ERRRDDPDHL TVRIGVADLP SGVTLDDPDL
LEHRRTVASP ARAVPVTVAL ADRGVVGLHG RTPERRALAA WMVAQLCVLQ SPRDLMVVVL
TDRDAEEHWG WLAWVPHARP DKGDADSRVR LGNDSESVAR RLTELAAVVD ARQRARRESS
GAVLDAPDVL VVVDGSRRLR ALPGLVTVLR DGPAVGVVAL CLDSDRRSLP EECVTVVQAG
RSAHELSAHR EADVQHVRVD ALPVGWHDSV ARALAPVVDV DDGGDAGGLP TSSRLLDVLG
LDRPSGRAVL ARWAERAPST EVLLGEGVDG PFSIDLRRDG PHALVAGTTG SGKSELLQSV
VASLAASNAP DSMTFVLVDY KGGAAFRDCG PLPHTVGMVT DLDPHLVQRA LTSLGAELHR
REQLLALAEA KDLEDYEEAR GRSEGGTLPT LPRLLIVIDE FASLARELPD FVTGLVNVAQ
RGRSLGIHLV LATQRPSGVV SSEIRANTNL RIALRVTDAG ESTDVIDAAD ASRIPRSAPG
RALVRLGAGA LVPFQAGRVG GRAERESRPD GTWSARLSWD GAAGPAPRPP ATAAVEDHET
TDLVQFVAAV VEAEALRGGE RPHRPWLDAL PALVELEHLV GAEAGGGGPP RTLPPLPFGL
EDHPREQARR TAALDLDVDG HLFVAGAARS GRSQVLRTLA ASIIRHTSSA DVHLYGIDCG
SGALLPLASA PHTGAVVRRT EVERARRLLA RLVEETLRRQ TVLAAGSWAS VTEQRRAAPE
EDRLPHVVLM IDPWEGFVAS LGDLDLGEPV ELVTLLLREG AAVGVHLVVT GDRLLVSGRM
ATLVERKLVL RMADRADYGL AGLDPRSMPD EPGPGRGADT VSGAETQVAV VGADPSGSAQ
AEALRQAAGE AVRRDLAVPP GRRPFRLDRL EGDLTFDGAW SRHDPAALGG AFAMVGIGGD
DLVPVGPRLA DAPGTFVVGG PPRSGRSTVL VSMVRSLLAQ GLEVVVVTPR SSPLRDLDGL
PGVVAVLRGP DLRSDELDAV LGDEAPEGRV LVVDDAELVK DAPAAAWLAD FVRSCADGPG
ALVAAGSAAD LGVGFMGWHA DLRRNRCGAV LSPRATSDGE LVGAQLARSA TSARSRPGRA
HVHLGDGVTV PVTVPRG
//
