ID   FLGI_SHESR              Reviewed;         363 AA.
AC   Q0HX20;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 68.
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};
GN   OrderedLocusNames=Shewmr7_1336;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000444; ABI42335.1; -; Genomic_DNA.
DR   RefSeq; WP_011625680.1; NC_008322.1.
DR   AlphaFoldDB; Q0HX20; -.
DR   SMR; Q0HX20; -.
DR   EnsemblBacteria; ABI42335; ABI42335; Shewmr7_1336.
DR   KEGG; shm:Shewmr7_1336; -.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; FTEQSFR; -.
DR   OrthoDB; 693640at2; -.
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; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           21..363
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_5000128727"
SQ   SEQUENCE   363 AA;  38323 MW;  7A3D1319BA4457CF CRC64;
     MKLKLILAVA MLAFSLPSQA ERIKDIANVQ GVRNNQLIGY GLVVGLPGTG EKTRYTEQTF
     TTMLKNFGIN LPDNFRPKIK NVAVVAVHAD MPAFIKPGQE LDVTVSSLGE AKSLRGGTLL
     QTFLKGVDGN VYAIAQGSLV VSGFSADGLD GSKVIQNTPT VGRIPNGAIV ERSVATPFST
     GDYLTFNLRR SDFSTAQRMA DAINDLLGPD MARPLDATSV QVSAPRDVSQ RVSFLATLEN
     IEVEPADESA KVIVNSRTGT IVVGQNVKLL PAAVTHGGLT VTIAEATQVS QPNALANGQT
     TVTSNSTINA SESNRRMFMF NPGTTLDELV RAVNLVGAAP SDVLAILEAL KVAGALHGEL
     III