FLGI_GLUOX
ID FLGI_GLUOX Reviewed; 380 AA.
AC Q5FT97;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=GOX0621;
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_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; CP000009; AAW60399.1; -; Genomic_DNA.
DR RefSeq; WP_011252198.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FT97; -.
DR SMR; Q5FT97; -.
DR STRING; 290633.GOX0621; -.
DR EnsemblBacteria; AAW60399; AAW60399; GOX0621.
DR KEGG; gox:GOX0621; -.
DR eggNOG; COG1706; Bacteria.
DR HOGENOM; CLU_045235_1_0_5; -.
DR OMA; VGPRDMI; -.
DR Proteomes; UP000006375; 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..35
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT CHAIN 36..380
FT /note="Flagellar P-ring protein"
FT /id="PRO_0000041796"
SQ SEQUENCE 380 AA; 39962 MW; 476DE7F487B8864A CRC64;
MRFFTQSPFP LRTLTRRLTA FVCVGLLLLP GFTLAASVRI KDITDMEGVR SNQLIGYGLV
VGLNGTGDRL TNTIFTRETL ISMLNRLGVN IRDQETQLQT HDVAAVMVTA DLPAFVHGGN
RIDVTVSAAG DASSLTGGTL LVTPLMAADG EVYAVAQGSL ATNAFSARGA AASITRNVPT
SGHIANGGIV EREVPFDLSH RANLHLSLRN PDFTTASRIA SIINRTFGPI AIVQDPRTVL
LDLSNHDPVS TLSRIGDLLV TPDTPAKVVV DEASGTIIMG ADVRISTVAV AQGNLTVQVT
ETPQVSQPGP FSGGQTAVVP RTNVKVDTGK THHLAVVPGG TTLRELVSGL NALGVGPRDM
ISILQAIKAD GALQAELEMR