ID   FLGI_PSET1              Reviewed;         364 AA.
AC   Q3IDW0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=PSHAa0776;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR954246; CAI85858.1; -; Genomic_DNA.
DR   RefSeq; WP_011327470.1; NC_007481.1.
DR   AlphaFoldDB; Q3IDW0; -.
DR   SMR; Q3IDW0; -.
DR   STRING; 326442.PSHAa0776; -.
DR   EnsemblBacteria; CAI85858; CAI85858; PSHAa0776.
DR   KEGG; pha:PSHAa0776; -.
DR   PATRIC; fig|326442.8.peg.739; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; FTEQSFR; -.
DR   OrthoDB; 693640at2; -.
DR   BioCyc; PHAL326442:PSHA_RS03785-MON; -.
DR   Proteomes; UP000006843; Chromosome I.
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..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           22..364
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000236309"
SQ   SEQUENCE   364 AA;  38380 MW;  60FFAA8D38ED8CE3 CRC64;
     MNVFKVFCLM VLLGWQLPAM AERIKDVSMV EGVRSNQLVG YGLVVGLPGT GEQSRFTEQS
     FKGMLNSFGI TLPASLKPKI KNVAAVAVHA ELPPFRKPGQ TIDITVSSIG SAGSLRGGTL
     LQTFLKGVDG NVYAIGQGSL IVGGLGAEGL DGSKVVINTP TVGRIPNGAT VERAVKSPFM
     QNDYITFNLN RPDFTTAKRL EKTINDLVGP NSAQALDAAS IRVIAPRDAS QRVSYLSTLE
     NLEFTPADTA AKIIVNSRTG TIVIGKNVKL QPAAITHGGL TVTIAEQLNV SQPNAFSDGD
     TVVTQQSIID IKQDDSRAFV FNPGVSLDDL VRAINEVGAA PGDLMAILEA LKEAGAINGQ
     LVVI