ID   FLGI_PECCP              Reviewed;         369 AA.
AC   C6D995;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 52.
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=PC1_2591;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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; CP001657; ACT13622.1; -; Genomic_DNA.
DR   RefSeq; WP_015840796.1; NC_012917.1.
DR   AlphaFoldDB; C6D995; -.
DR   SMR; C6D995; -.
DR   STRING; 561230.PC1_2591; -.
DR   EnsemblBacteria; ACT13622; ACT13622; PC1_2591.
DR   KEGG; pct:PC1_2591; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; KTIQITR; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000002736; 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; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           24..369
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_5000485719"
SQ   SEQUENCE   369 AA;  38243 MW;  04804524441C50C9 CRC64;
     MRIASFFTVL LTLLTLNIAP ASAERIRDLV NIQGVRGNAL IGYGLVVGLD GSGDQTMQTP
     FTTQSLTNML SQLGITVPAG TNMQLKNVAA VMVTAELPPF GRAGQNIDVV VSSLGNAKSL
     RGGTLLMTPL KGVDNQVYAL AQGNVLVGGA GASAGGSSVQ VNQLAGGRIS NGAVIERELP
     STFGASNTIM LQLKNDDFSM AQKVSDAINR SGYGGTATPL DSRTIQVLAP HGNSSQVRFL
     ADVQNIEVNV GIQDAKVVIN SRTGSVVMNR DVTLDSCAIA QGNLSVTINQ QANVSQPNTP
     FGGGQTVVTP QTEISVQQAG GALQRVNSSA NLNNVVRALN SLGATPMELM SILQAMQSAG
     CLRAKLEII