ID A0A268SIR0_9BACL Unreviewed; 451 AA.
AC A0A268SIR0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Flagellar biosynthesis protein FlhF {ECO:0000256|ARBA:ARBA00014919};
DE AltName: Full=Flagella-associated GTP-binding protein {ECO:0000256|ARBA:ARBA00030866};
GN Name=flhF {ECO:0000313|EMBL:PAF32257.1};
GN ORFNames=CHI14_07470 {ECO:0000313|EMBL:PAF32257.1};
OS Paenibacillus sp. 7516.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2022549 {ECO:0000313|EMBL:PAF32257.1, ECO:0000313|Proteomes:UP000216732};
RN [1] {ECO:0000313|EMBL:PAF32257.1, ECO:0000313|Proteomes:UP000216732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7516 {ECO:0000313|EMBL:PAF32257.1,
RC ECO:0000313|Proteomes:UP000216732};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Necessary for flagellar biosynthesis. May be involved in
CC translocation of the flagellum. {ECO:0000256|ARBA:ARBA00025337}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family.
CC {ECO:0000256|ARBA:ARBA00008531}.
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:PAF32257.1}.
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DR EMBL; NPBI01000007; PAF32257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268SIR0; -.
DR Proteomes; UP000216732; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd17873; FlhF; 1.
DR Gene3D; 1.20.120.1380; Flagellar FlhF biosynthesis protein, N domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR020006; FlhF.
DR InterPro; IPR047040; FlhF__GTPase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR NCBIfam; TIGR03499; FlhF; 1.
DR PANTHER; PTHR43134:SF3; FLAGELLAR BIOSYNTHESIS PROTEIN FLHF; 1.
DR PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR Pfam; PF00448; SRP54; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795};
KW Bacterial flagellum protein export {ECO:0000256|ARBA:ARBA00023225};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000313|EMBL:PAF32257.1};
KW Cilium {ECO:0000313|EMBL:PAF32257.1};
KW Flagellum {ECO:0000313|EMBL:PAF32257.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 255..401
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 256..447
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|SMART:SM00962"
FT REGION 100..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 50856 MW; 00A74599B48CC0C8 CRC64;
MRVKQYIVET MPEAMLQIRK DLGSNAVILS TKEIKVGGMM GMFRKKRIEV VAAVEEEDKK
EAKKQIQNQV ASVPRSYVPE AYRQTARSFV NEANQSESAA QVVEQRADEK RKETAAHAES
INIESDRGYG KFESSMDYKP RPEGADFSGS SSPSVQEPNK QGQQELMSEL KELKKMMTQL
SRQNELADPV PEEFLFLRER LINQEVRAEV FESWFETVQT QLNAKELDEN EIVQSVQKQI
LTFLEERIDA GILPGTRIVY VAGPTGVGKT TTIAKLAAEQ MFKHHRKVGF ITSDTYRISA
VEQLRTYASI LNVPLEVVQS PGDTQRAISR LQDCDLIFMD TAGRNYRNEL LVSELQSLLA
PVENSETFLV MSMTSKSADM FEITEHFSKY GLDKIIFTKM DETGTCGPMI NLLHHFPLKL
AYVTNGQNVP DDLLKPDPAS LTKQLLGELA K
//
