ID   FLGH_BUCA5              Reviewed;         238 AA.
AC   B8D9C9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Flagellar L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE   AltName: Full=Basal body L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE   Flags: Precursor;
GN   Name=flgH {ECO:0000255|HAMAP-Rule:MF_00415}; OrderedLocusNames=BUAP5A_337;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=563178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5A;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
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:0000255|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:0000255|HAMAP-Rule:MF_00415}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00415}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00415}.
CC       Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00415}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00415}.
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DR   EMBL; CP001161; ACL30700.1; -; Genomic_DNA.
DR   RefSeq; WP_009874298.1; NC_011833.1.
DR   AlphaFoldDB; B8D9C9; -.
DR   SMR; B8D9C9; -.
DR   KEGG; bap:BUAP5A_337; -.
DR   HOGENOM; CLU_069313_0_0_6; -.
DR   OMA; ITQQPMT; -.
DR   OrthoDB; 1900876at2; -.
DR   Proteomes; UP000006904; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           24..238
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_1000134826"
FT   LIPID           24
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   LIPID           24
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ   SEQUENCE   238 AA;  26125 MW;  E30D0A05754CFB14 CRC64;
     MIKLFICQKK YYLTAIFLLT IQSCASVEYK PLVTGATTAI APNIWPKVVN GSLFQEKIPI
     NYGYQPLFED HRPHNIGDTI TVVLQENISA SNSSISNMSR DGSANFGLKI APGQLNNILG
     VNFQDNTTSL DSFGRNNFSG KGSNSANNKF TGLITVTVKR VLPNGNLKVI GEKQVSINKG
     TEFIRFSGVI NPTNINKNNF ISSTQIADAR IEYLSHGGLD DVQKMGWLQK LLLKISPI