ID A0A0Q7K087_9ACTN Unreviewed; 1377 AA.
AC A0A0Q7K087;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=FHA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASD06_08455 {ECO:0000313|EMBL:KQX65652.1};
OS Angustibacter sp. Root456.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae.
OX NCBI_TaxID=1736539 {ECO:0000313|EMBL:KQX65652.1, ECO:0000313|Proteomes:UP000051170};
RN [1] {ECO:0000313|EMBL:KQX65652.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX65652.1,
RC ECO:0000313|Proteomes:UP000051170};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX65652.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX65652.1,
RC ECO:0000313|Proteomes:UP000051170};
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:KQX65652.1}.
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DR EMBL; LMER01000016; KQX65652.1; -; Genomic_DNA.
DR RefSeq; WP_056676710.1; NZ_LMER01000016.1.
DR STRING; 1736539.ASD06_08455; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000051170; 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; IPR000253; FHA_dom.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR032030; YscD_cytoplasmic_dom.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR PANTHER; PTHR22683:SF1; TYPE VII SECRETION SYSTEM PROTEIN ESSC; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR Pfam; PF16697; Yop-YscD_cpl; 1.
DR SMART; SM00382; AAA; 3.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50901; FTSK; 1.
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051170};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 111..160
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 599..791
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 833..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 617..624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1377 AA; 143918 MW; ADF5169F97482FC1 CRC64;
MISLRCTVVR ADRPCDPCDV EVEAPDGSTA ADLVRALVGA GITDAPTSLS TGGAAIAATT
PLGRRPLVHG ALLVAARTWP TDLHTPRSTL ALHVVSGPDA GTVLPLSAGS TTVGRGASAS
LDVADPLLSR RHYELRLGSG GLTLHDLGSS NGTLVEGSPL PAGGVECPPG TRILAGGTTF
AVRTPSSRPA AQRDTGDGFV AVTRGPRTAA APVGVRFRRR PPPQPAEHAP WPWIAMLAPL
LLCAPLAWFT RQPTYLALGL MSPLTMGVSQ LVERRGRRRR DHEQHAAWQA GDRRTCALVD
QAVAADLALR RAAFPDPALL LETARLPGHR LWERGPDDSD LLQVALGCGD VPSEVEVQTE
DGATRPVLAN APVVLDLAEA GHLGVSGSPD AVGGVLRLLV AQLAVQCSPR AVRVVALDDD
GRWTRWLPHH RHDTPAGLAH EVRRRLELVS GPAGPPLSPR LVVVAHDVAA WASDPSFAVL
LDDGPRAGVH VVAGAALAEQ LPSRCDAVLT IADRQPSTLT RRDGRSAELV VDAVAEVWAL
EVARALAPLR DATPEPGRLP DRVLLADVCG FDPSSADDVA SAWRRSPRTT RAVIGAGEDG
PVHVDLLRDG PHALVAGTTG AGKSELLQTL VCSLALGNRP DELAFVLVDY KGGAAFRELS
DLPHVAGLVT DLDAHLADRA LASLQAELTR RERLFASVGA SDFTGYLALR DTGRAPEPLA
RLVLVVDEFR LLADELPGFL DGLVRLASIG RSLGVHLVLA TQRPAGVVTA DIKANVNLRI
CLRVRDRAES DDVVDVPDAA LLPVDVPGRA VLRTGSDALV PVQVALVAEP TDGASPQTVS
VRPLALGTPS RTGPTTTGAG RGRVSNSGAG PWPLVRALQQ AAAACRAVPP PSPWLPPLPD
LVLPADLVAG TPAATSVPYA IADRPDLGER HQLVWDATTS SHLAVCGMAR TGKSTACIAL
ALAACEQLSA DDLHVHVIEG SPRVGPALAD LPHLGTTTVS SQPAAVARLV QRLLREPPRS
PHTLLLVDGW EAVAESLDAR DHGRTTDELL GLLRDGERWG LRAVVTGGRA VLSARVSALL
PERLMLRTAD PTDLLLAGAA SPSPLTHQPP GRAVHLPAGH EVQVVWSGDD AEVRRRVQAV
REQHAGRTSA TQPLRLRALP HHAELTADGE GHPTGLGVRV GVGGDEVEAM QLDVSCAPVV
TVAGPAGSGR SSTLASWAAQ LHERAVGVLA VADSTSPLAH GPWPVRDPLR LADSEPAPGV
ACLLVDDVDR LPDAVVGRLL AWTSWASPGR ALVVASTTDA LTSSFTGLAA AVRRHRTGVL
LQPERPLDGD VFGVAAERPD VRTPGRGLLV VRGRATPVQV ALPQAAAPRT EKWGTAS
//
