FLGH_BORPE
ID FLGH_BORPE Reviewed; 229 AA.
AC Q7VYG3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Flagellar L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE AltName: Full=Basal body L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE Flags: Precursor;
GN Name=flgH {ECO:0000255|HAMAP-Rule:MF_00415}; OrderedLocusNames=BP1379;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
CC -!- FUNCTION: Assembles around the rod to form the L-ring and probably
CC protects the motor/basal body from shearing forces during rotation.
CC {ECO:0000255|HAMAP-Rule:MF_00415}.
CC -!- SUBUNIT: The basal body constitutes a major portion of the flagellar
CC organelle and consists of four rings (L,P,S, and M) mounted on a
CC central rod. {ECO:0000255|HAMAP-Rule:MF_00415}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00415}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00415}.
CC Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00415}.
CC -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000255|HAMAP-
CC Rule:MF_00415}.
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DR EMBL; BX640415; CAE41670.1; -; Genomic_DNA.
DR RefSeq; NP_880126.1; NC_002929.2.
DR RefSeq; WP_010930326.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VYG3; -.
DR SMR; Q7VYG3; -.
DR STRING; 257313.BP1379; -.
DR KEGG; bpe:BP1379; -.
DR PATRIC; fig|257313.5.peg.1480; -.
DR eggNOG; COG2063; Bacteria.
DR HOGENOM; CLU_069313_0_0_4; -.
DR OMA; ITQQPMT; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0009427; C:bacterial-type flagellum basal body, distal rod, L ring; IEA:InterPro.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR HAMAP; MF_00415; FlgH; 1.
DR InterPro; IPR000527; Flag_Lring.
DR PANTHER; PTHR34933; PTHR34933; 1.
DR Pfam; PF02107; FlgH; 1.
DR PRINTS; PR01008; FLGLRINGFLGH.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT CHAIN 21..229
FT /note="Flagellar L-ring protein"
FT /id="PRO_0000009425"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ SEQUENCE 229 AA; 24122 MW; 631E6652A5EADE54 CRC64;
MLKTVLRLPV CAALLALAAG CAMIPPEPVV ICPLTAPPPS PPQPSARPNG SIYQPSAYGN
YPLFEDRRPR NVGDIVTIVL EEKTNAAKGV ATNTSRDGSA TLGVAAAPRF MDGIINDKLD
TDISGGNTAN GTGKSSANNT FTGTITTTVI GVLPNGNLQI AGEKQIAINR GSEYVRFSGV
VDPRSITGSN TVSSTRVADA RIEYRSKGVM DEVQTMGWLQ RFFLIASPF