FLHF_BACSU
ID FLHF_BACSU Reviewed; 366 AA.
AC Q01960;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Flagellar biosynthesis protein FlhF;
DE AltName: Full=Flagella-associated GTP-binding protein;
GN Name=flhF; OrderedLocusNames=BSU16400;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1447978; DOI=10.1111/j.1365-2958.1992.tb01447.x;
RA Carpenter P.B., Hanlon D.W., Ordal G.W.;
RT "flhF, a Bacillus subtilis flagellar gene that encodes a putative GTP-
RT binding protein.";
RL Mol. Microbiol. 6:2705-2713(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Necessary for flagellar biosynthesis. May be involved in
CC translocation of the flagellum.
CC -!- INTERACTION:
CC Q01960; Q01960: flhF; NbExp=2; IntAct=EBI-15652472, EBI-15652472;
CC Q01960; P40742: ylxH; NbExp=9; IntAct=EBI-15652472, EBI-15950871;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. {ECO:0000305}.
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; X66445; CAA47062.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13513.1; -; Genomic_DNA.
DR PIR; S25277; S25277.
DR RefSeq; NP_389522.1; NC_000964.3.
DR RefSeq; WP_003231945.1; NZ_JNCM01000035.1.
DR PDB; 2PX0; X-ray; 3.00 A; A/B/C/D/E/F/G/H=79-366.
DR PDB; 2PX3; X-ray; 3.20 A; A=79-366.
DR PDB; 3SYN; X-ray; 3.06 A; A/B/C/D=79-366.
DR PDBsum; 2PX0; -.
DR PDBsum; 2PX3; -.
DR PDBsum; 3SYN; -.
DR AlphaFoldDB; Q01960; -.
DR SMR; Q01960; -.
DR DIP; DIP-46493N; -.
DR IntAct; Q01960; 1.
DR STRING; 224308.BSU16400; -.
DR PaxDb; Q01960; -.
DR PRIDE; Q01960; -.
DR EnsemblBacteria; CAB13513; CAB13513; BSU_16400.
DR GeneID; 940021; -.
DR KEGG; bsu:BSU16400; -.
DR PATRIC; fig|224308.179.peg.1781; -.
DR eggNOG; COG1419; Bacteria.
DR InParanoid; Q01960; -.
DR OMA; WYEVDEY; -.
DR PhylomeDB; Q01960; -.
DR BioCyc; BSUB:BSU16400-MON; -.
DR EvolutionaryTrace; Q01960; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005047; F:signal recognition particle binding; IBA:GO_Central.
DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR020006; FlhF.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR PANTHER; PTHR43134:SF3; PTHR43134:SF3; 2.
DR Pfam; PF00448; SRP54; 1.
DR SMART; SM00962; SRP54; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03499; FlhF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum biogenesis;
KW Bacterial flagellum protein export; Cell membrane; GTP-binding; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT CHAIN 1..366
FT /note="Flagellar biosynthesis protein FlhF"
FT /id="PRO_0000101220"
FT REGION 64..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 182..189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 259..263
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 317..320
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:2PX0"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:2PX0"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2PX0"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:2PX0"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:2PX0"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2PX0"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:2PX0"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:2PX0"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:2PX0"
FT HELIX 219..227
FT /evidence="ECO:0007829|PDB:2PX0"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:2PX0"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3SYN"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:2PX0"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:2PX0"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:2PX0"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:2PX0"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:2PX0"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:2PX0"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:2PX0"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:2PX0"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:2PX0"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:2PX0"
FT HELIX 326..333
FT /evidence="ECO:0007829|PDB:2PX0"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:2PX0"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:2PX0"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:3SYN"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:2PX0"
SQ SEQUENCE 366 AA; 41150 MW; E5A3577E49D16F1C CRC64;
MKIKKFTAAS MQEAALLIRK ELGNEAVILN SKKIKKRKWF GLVNKPAVEV IAVLDQDFLE
KKTPQKAAEP KQTLKTPVSS PKIEERTYPP QIPAQQELGD FSAYQSVLPE PLRKAEKLLQ
ETGIKESTKT NTLKKLLRFS VEAGGLTEEN VVGKLQEILC DMLPSADKWQ EPIHSKYIVL
FGSTGAGKTT TLAKLAAISM LEKHKKIAFI TTDTYRIAAV EQLKTYAELL QAPLEVCYTK
EEFQQAKELF SEYDHVFVDT AGRNFKDPQY IDELKETIPF ESSIQSFLVL SATAKYEDMK
HIVKRFSSVP VNQYIFTKID ETTSLGSVFN ILAESKIGVG FMTNGQNVPE DIQTVSPLGF
VRMLCR
