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Database: UniProt
Entry: H0BWE7_9BURK
LinkDB: H0BWE7_9BURK
Original site: H0BWE7_9BURK 
ID   H0BWE7_9BURK            Unreviewed;       503 AA.
AC   H0BWE7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Flagellar biosynthesis protein FlhF {ECO:0000256|ARBA:ARBA00014919};
DE   AltName: Full=Flagella-associated GTP-binding protein {ECO:0000256|ARBA:ARBA00030866};
GN   ORFNames=KYG_08570 {ECO:0000313|EMBL:EHL23290.1};
OS   Acidovorax sp. NO-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL23290.1, ECO:0000313|Proteomes:UP000003485};
RN   [1] {ECO:0000313|EMBL:EHL23290.1, ECO:0000313|Proteomes:UP000003485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NO-1 {ECO:0000313|EMBL:EHL23290.1,
RC   ECO:0000313|Proteomes:UP000003485};
RX   PubMed=22374962; DOI=10.1128/JB.06814-11;
RA   Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT   "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT   Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL   J. Bacteriol. 194:1635-1636(2012).
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}.
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DR   EMBL; AGTS01000072; EHL23290.1; -; Genomic_DNA.
DR   RefSeq; WP_008904409.1; NZ_AGTS01000072.1.
DR   AlphaFoldDB; H0BWE7; -.
DR   STRING; 512030.KYG_08570; -.
DR   PATRIC; fig|512030.4.peg.1671; -.
DR   OrthoDB; 9778554at2; -.
DR   Proteomes; UP000003485; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000003485};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          273..441
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          274..464
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00962"
FT   REGION          51..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  54988 MW;  FCA3B2B449B22BEB CRC64;
     MNIKRFTAPT SREALAKARM AFGDGTLILS NRPTANGVEV VATAEDTLSA LDGGAAPSSN
     PPLLAPKPAR TAPQRASQPA ASTLDRNPVE EDTEQLAMST LSFQDYVRER MLRRRHEALN
     GPAEPQTLSE RSRDQEPERE RMPAPAVVRH NPLRSIPMDI PPEPPRRRQE AVSTHLAASN
     SNQQSVMNEL HAVKELIEDR FNTLAWLGQA RQNPIQSNLM LKMIRAGYSP SLARAVLERM
     PEDLSAAESV RWLMEVLERN LKTDQAEAPL YEQGGIFAMV GSTGVGKTTT TAKLAALCAR
     IHGPGSVGLI TLDTYRVGAH EQLRSYGRML GIVAHLAHDR AALQDLLGLL SGKKMVLIDT
     TGVAPRDPRK RDMLDVLDLP HVNRLLVLNA GCHGDTLDDV LTAFKTEGSQ QAILSKVDEA
     VKLGPAIDAL IRHQMVLRGV TNGQRVPEDW ERADAHKLIS TSMRAPAKSA FDPKATDLNF
     FFSHSPDSVG VNMNMNERGL VDA
//
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