FLGH_GLUOX
ID FLGH_GLUOX Reviewed; 248 AA.
AC Q5FRE4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=GOX1291;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW61052.1; -; Genomic_DNA.
DR RefSeq; WP_011252844.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FRE4; -.
DR STRING; 290633.GOX1291; -.
DR EnsemblBacteria; AAW61052; AAW61052; GOX1291.
DR GeneID; 56905602; -.
DR KEGG; gox:GOX1291; -.
DR eggNOG; COG2063; Bacteria.
DR HOGENOM; CLU_069313_1_2_5; -.
DR OMA; QARISYG; -.
DR Proteomes; UP000006375; 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 Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT CHAIN 24..248
FT /note="Flagellar L-ring protein"
FT /id="PRO_0000009448"
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 248 AA; 26598 MW; DCE71BA33034B83D CRC64;
MRHAFRHSVR TLGLLGLLPV LSACNSLAQM SEIGRPPRMT SITDPTLANS YRPVTMPMPP
LQAPPDEAAS LWRSGSKAFF KDQRASQVGD LVTIIVDITD NAAFNNGTTA DRTADEKFGI
PNLFGIKGKV ISAITGADSL STASSSDSGA TGKITRNETV TLRLAGTITQ VLPNGNFVVM
GKQEVRVNSE LRELGVSGIV RPQDITADNT VTHDRMAEAR ISYGGRGTLT QLQTPRYGQQ
VMDAILPF