ID   E5B4B7_ERWAM            Unreviewed;       233 AA.
AC   E5B4B7;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   03-MAY-2023, entry version 37.
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:CBX80320.1};
GN   ORFNames=EAIL5_1500 {ECO:0000313|EMBL:CBX80320.1};
OS   Erwinia amylovora ATCC BAA-2158.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=889211 {ECO:0000313|EMBL:CBX80320.1};
RN   [1] {ECO:0000313|EMBL:CBX80320.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-2158 {ECO:0000313|EMBL:CBX80320.1};
RA   Powney R., Smits T.H., Sawbridge T., Frey B., Blom J., Frey J.E.,
RA   Plummer K.M., Beer S.V., Luck J., Duffy B., Rodoni B.;
RT   "Genome Sequence of an Erwinia amylovora Strain with Pathogenicity
RT   Restricted to Rubus Plants.";
RL   J. Bacteriol. 193:785-786(2011).
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}. Bacterial flagellum basal body {ECO:0000256|HAMAP-
CC       Rule:MF_00415}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000256|ARBA:ARBA00006929,
CC       ECO:0000256|HAMAP-Rule:MF_00415}.
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DR   EMBL; FR719190; CBX80320.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5B4B7; -.
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.
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:CBX80320.1};
KW   Cilium {ECO:0000313|EMBL:CBX80320.1};
KW   Flagellum {ECO:0000313|EMBL:CBX80320.1};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ   SEQUENCE   233 AA;  24638 MW;  3C8F3A30F736C697 CRC64;
     MARQISLSGR WLVATLLLTL NGCALVPRKP LVEGSTTAQP LPASPAMVNG SIFQGVMPMN
     YGYQPLFEDR RPRNIGDTLT ITLQENVSAS KSSSANAGRD GSAEFGLTAT PRALVGLLGG
     DKANLGGSGK NDFEGKGGAT AKNTFTGTIT VTVNQVLPNG NLNVVGEKQI EINQGTEFIR
     FSGVVNPRTI SASNSVVSSQ VADARIEYVG NGYINEAQTM GWLQRFFLNI SPM
//