ID   FLGH_PECAS              Reviewed;         237 AA.
AC   Q6D6H3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Flagellar L-ring protein;
DE   AltName: Full=Basal body L-ring protein;
DE   Flags: Precursor;
GN   Name=flgH; OrderedLocusNames=ECA1708;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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:0000250}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG74614.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX950851; CAG74614.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_039292566.1; NC_004547.2.
DR   AlphaFoldDB; Q6D6H3; -.
DR   SMR; Q6D6H3; -.
DR   STRING; 218491.ECA1708; -.
DR   DNASU; 2881851; -.
DR   EnsemblBacteria; CAG74614; CAG74614; ECA1708.
DR   GeneID; 57209579; -.
DR   KEGG; eca:ECA1708; -.
DR   PATRIC; fig|218491.5.peg.1735; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_0_0_6; -.
DR   OrthoDB; 1900876at2; -.
DR   Proteomes; UP000007966; 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.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..237
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000009446"
FT   LIPID           27
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           27
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   237 AA;  25119 MW;  B9D34C317CF5E9DA CRC64;
     MNAKSVIKPL RRPRLLALIA MLALNGCAYI PHDKVVTGPT TAQPGSPVLA GPNGSIFQTV
     QPMNYGYQPM FEDRRPRNIG DTLTIVLQEN VSASKSSSAN AARNGSSTFG VATTPRYLEG
     PLGNNRAALD ATGTNDFSGK GGANANNTFS GTITVTVGQV LANGNLNVVG EKQIAINQGT
     EFIRFSGVVN PRTISGNNSV PSTQVADARI EYVGNGYINE AQNMGWLQRF FLNVSPF