ID A0A0E8EFU5_BORPT Unreviewed; 229 AA.
AC A0A0E8EFU5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Flagellar L-ring protein {ECO:0000256|HAMAP-Rule:MF_00415};
DE AltName: Full=Basal body L-ring protein {ECO:0000256|HAMAP-Rule:MF_00415};
GN Name=flgH {ECO:0000256|HAMAP-Rule:MF_00415,
GN ECO:0000313|EMBL:SUV64695.1};
GN ORFNames=NCTC10911_01726 {ECO:0000313|EMBL:SUV64695.1};
OS Bordetella pertussis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=520 {ECO:0000313|EMBL:SUV64695.1, ECO:0000313|Proteomes:UP000255014};
RN [1] {ECO:0000313|EMBL:SUV64695.1, ECO:0000313|Proteomes:UP000255014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10911 {ECO:0000313|EMBL:SUV64695.1,
RC ECO:0000313|Proteomes:UP000255014};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002591, ECO:0000256|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:0000256|ARBA:ARBA00011439, ECO:0000256|HAMAP-
CC Rule:MF_00415}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_00415}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_00415}.
CC Bacterial flagellum basal body {ECO:0000256|HAMAP-Rule:MF_00415}.
CC -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000256|ARBA:ARBA00006929,
CC ECO:0000256|HAMAP-Rule:MF_00415}.
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DR EMBL; UFTT01000002; SUV64695.1; -; Genomic_DNA.
DR RefSeq; WP_010930326.1; NZ_UIGD01000006.1.
DR AlphaFoldDB; A0A0E8EFU5; -.
DR SMR; A0A0E8EFU5; -.
DR GeneID; 69601290; -.
DR OMA; WFDRFFL; -.
DR Proteomes; UP000255014; Unassembled WGS sequence.
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; FLAGELLAR L-RING PROTEIN; 1.
DR PANTHER; PTHR34933:SF3; FLAGELLAR L-RING PROTEIN; 1.
DR Pfam; PF02107; FlgH; 1.
DR PRINTS; PR01008; FLGLRINGFLGH.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143, ECO:0000256|HAMAP-
KW Rule:MF_00415}; Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_00415};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|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
//
