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Database: UniProt
Entry: D8ISY0_HERSS
LinkDB: D8ISY0_HERSS
Original site: D8ISY0_HERSS 
ID   D8ISY0_HERSS            Unreviewed;       219 AA.
AC   D8ISY0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
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:ADJ63539.1};
GN   OrderedLocusNames=Hsero_2039 {ECO:0000313|EMBL:ADJ63539.1};
OS   Herbaspirillum seropedicae (strain SmR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ63539.1, ECO:0000313|Proteomes:UP000000329};
RN   [1] {ECO:0000313|EMBL:ADJ63539.1, ECO:0000313|Proteomes:UP000000329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SmR1 {ECO:0000313|EMBL:ADJ63539.1,
RC   ECO:0000313|Proteomes:UP000000329};
RA   Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B.,
RA   Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F.,
RA   Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E.,
RA   Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G.,
RA   Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O.,
RA   Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G.,
RA   Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C.,
RA   Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA   Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA   Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA   Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA   Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P.,
RA   Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C.,
RA   Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M.,
RA   Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K.,
RA   Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E.,
RA   Weiss V.A., Yates M.A., Souza E.M.;
RT   "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-
RT   fixing, plant-growth promoting beta-Proteobacteria.";
RL   Submitted (APR-2010) 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; CP002039; ADJ63539.1; -; Genomic_DNA.
DR   RefSeq; WP_013234025.1; NC_014323.1.
DR   AlphaFoldDB; D8ISY0; -.
DR   STRING; 757424.Hsero_2039; -.
DR   KEGG; hse:Hsero_2039; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_0_0_4; -.
DR   OrthoDB; 9789463at2; -.
DR   Proteomes; UP000000329; 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; 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   Cell projection {ECO:0000313|EMBL:ADJ63539.1};
KW   Cilium {ECO:0000313|EMBL:ADJ63539.1};
KW   Flagellum {ECO:0000313|EMBL:ADJ63539.1};
KW   Lipoprotein {ECO:0000256|HAMAP-Rule:MF_00415};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000329};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00415}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..219
FT                   /note="Flagellar L-ring protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008952775"
SQ   SEQUENCE   219 AA;  22798 MW;  ED765A02FED82AC2 CRC64;
     MKSMLKWVTL AGILAVAGCT TVPDSIVAGP KSARPQPASY APPTSGAIFQ GAVYRPLLED
     RRARLVGDTL TIVINEKTSA GKSAASSASK TGAVNSPVPT FFGTSIKELT ANGSSSAKFD
     DKGATTSSNT FTGTIGVTVV EVLPNGNLVV AGEKQVALDK GVEYVRFSGT VSPDNIQTGN
     TVSSTLVADA KVEYRTNTRV DMADFMSSLG RFFFSISPF
//
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