FLGH_SALPA
ID FLGH_SALPA Reviewed; 232 AA.
AC Q5PGU6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=SPA1671;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(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: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; CP000026; AAV77596.1; -; Genomic_DNA.
DR RefSeq; WP_001174897.1; NC_006511.1.
DR AlphaFoldDB; Q5PGU6; -.
DR SMR; Q5PGU6; -.
DR EnsemblBacteria; AAV77596; AAV77596; SPA1671.
DR KEGG; spt:SPA1671; -.
DR HOGENOM; CLU_069313_0_0_6; -.
DR OMA; ITQQPMT; -.
DR Proteomes; UP000008185; 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..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT CHAIN 22..232
FT /note="Flagellar L-ring protein"
FT /id="PRO_0000009469"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ SEQUENCE 232 AA; 24709 MW; A555EEF7BAB55E36 CRC64;
MQKYALHAYP VMALMVATLT GCAWIPAKPL VQGATTAQPI PGPVPVANGS IFQSAQPINY
GYQPLFEDRR PRNIGDTLTI VLQENVSASK SSSANASRDG KTSFGFDTVP RYLQGLFGNS
RADMEASGGN SFNGKGGANA SNTFSGTLTV TVDQVLANGN LHVVGEKQIA INQGTEFIRF
SGVVNPRTIS GSNSVPSTQV ADARIEYVGN GYINEAQNMG WLQRFFLNLS PM
