FLGI_SULDN
ID FLGI_SULDN Reviewed; 351 AA.
AC Q30T40;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Flagellar P-ring protein {ECO:0000255|HAMAP-Rule:MF_00416};
DE AltName: Full=Basal body P-ring protein {ECO:0000255|HAMAP-Rule:MF_00416};
DE Flags: Precursor;
GN Name=flgI {ECO:0000255|HAMAP-Rule:MF_00416}; OrderedLocusNames=Suden_0562;
OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS denitrificans (strain ATCC 33889 / DSM 1251)).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Thiovulaceae; Sulfurimonas.
OX NCBI_TaxID=326298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33889 / DSM 1251;
RX PubMed=18065616; DOI=10.1128/aem.01844-07;
RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT denitrificans.";
RL Appl. Environ. Microbiol. 74:1145-1156(2008).
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_00416}.
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_00416}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00416}.
CC Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00416}.
CC -!- SIMILARITY: Belongs to the FlgI family. {ECO:0000255|HAMAP-
CC Rule:MF_00416}.
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DR EMBL; CP000153; ABB43841.1; -; Genomic_DNA.
DR RefSeq; WP_011372195.1; NC_007575.1.
DR AlphaFoldDB; Q30T40; -.
DR SMR; Q30T40; -.
DR STRING; 326298.Suden_0562; -.
DR EnsemblBacteria; ABB43841; ABB43841; Suden_0562.
DR KEGG; tdn:Suden_0562; -.
DR eggNOG; COG1706; Bacteria.
DR HOGENOM; CLU_045235_1_0_7; -.
DR OMA; KTIQITR; -.
DR OrthoDB; 693640at2; -.
DR Proteomes; UP000002714; Chromosome.
DR GO; GO:0009428; C:bacterial-type flagellum basal body, distal rod, P ring; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR HAMAP; MF_00416; FlgI; 1.
DR InterPro; IPR001782; Flag_FlgI.
DR PANTHER; PTHR30381; PTHR30381; 1.
DR Pfam; PF02119; FlgI; 1.
DR PRINTS; PR01010; FLGPRINGFLGI.
PE 3: Inferred from homology;
KW Bacterial flagellum; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT CHAIN 21..351
FT /note="Flagellar P-ring protein"
FT /id="PRO_0000236325"
SQ SEQUENCE 351 AA; 37636 MW; EEE26263B4B8D505 CRC64;
MKKILFLFTA SLLLHVTLQA AKISDVASIV GVRDNHLIGY SLVVGLQKTG DGTTSKFTLQ
SIANMLKAMN IDMKPIDIKS KNVAAVVVTA ELAPFARQGD KINITVSSIG DAKSLEGGTL
LMTPLKGVDG KIYALAQGAV SIGGRNGKGA GDSHPTAGLI YDGGLVEREI AIDLYNQDYV
TLSLKDANFQ NSVSIQKTLN GYYSTEVAVA MDSRTVKLKK PSNKTMIEFL AEVQEINMDY
NVQDRIVINE RTGTIISGVG IHIKPIIMTH GDITIKITEQ ENPDKPAGSM VVDENMVIGL
NENELYTKEG TTTVANLVRS LQKLGATPKD IISILEAMKS AGSISAELKL I