ID A0A0P1FBP1_9RHOB Unreviewed; 243 AA.
AC A0A0P1FBP1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:CUH51359.1};
GN ORFNames=SHM7688_00795 {ECO:0000313|EMBL:CUH51359.1};
OS Shimia marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH51359.1, ECO:0000313|Proteomes:UP000054823};
RN [1] {ECO:0000313|EMBL:CUH51359.1, ECO:0000313|Proteomes:UP000054823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH51359.1,
RC ECO:0000313|Proteomes:UP000054823};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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|HAMAP-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; CYPW01000006; CUH51359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1FBP1; -.
DR STRING; 321267.SHM7688_00795; -.
DR OrthoDB; 9789227at2; -.
DR Proteomes; UP000054823; 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:SF1; 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};
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW Rule:MF_00415}; Lipoprotein {ECO:0000256|HAMAP-Rule:MF_00415};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW Reference proteome {ECO:0000313|Proteomes:UP000054823};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00415}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..243
FT /note="Flagellar L-ring protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008848680"
FT REGION 96..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 243 AA; 26416 MW; 92FE555C7B05F069 CRC64;
MRFISALLVL SALALSGCAR TDHIGKAPSF TPTTNNQEHY AMMNPPLPTQ ASVSRRSDTA
SLWSRNRQSL LGDRRAASRG DILTVVIEVD EKAQIDNESE RNRSGSETLS VPQLIGLPQR
LNSKLPDGAT TDPLVDLSSD SKSSGDGSVK RSEKLTLRVA ATVVDVLPNG VLAIQGTQEL
RVNFELRELL VSGYVRSEDV SRQNEITFDK IASARVSYGG RGQITDMQQP RVGQQVLDAV
LPF
//