ID   FLGI_DESDA              Reviewed;         370 AA.
AC   B8J2Y1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=Ddes_2004;
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 / DSM 6949 / MB;
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., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT   ATCC 27774.";
RL   Submitted (JAN-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; CP001358; ACL49900.1; -; Genomic_DNA.
DR   RefSeq; WP_012625624.1; NC_011883.1.
DR   AlphaFoldDB; B8J2Y1; -.
DR   SMR; B8J2Y1; -.
DR   STRING; 525146.Ddes_2004; -.
DR   EnsemblBacteria; ACL49900; ACL49900; Ddes_2004.
DR   KEGG; dds:Ddes_2004; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_7; -.
DR   OMA; KTIQITR; -.
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..28
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           29..370
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_5000432117"
FT   REGION          295..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  39106 MW;  99AED6AF48D13FD7 CRC64;
     MKLTILRHPV LWIFTAALLL SMVLPAQAVR IKDIASFSGV RDNQLIGYGL VVGLAGTGDK
     KDAVFTLSSM KNMMDRMGIG VDSSALKTKN VASVMVTARM PVSAKPGTRL DVTVSSVGDA
     TSLLGGVLLQ TALKGVDGKI YTLAQGSLTV GGFSSQGRAA SVSKNISTVG IIPGGGIVER
     GIPFEFNQQD KLTLHLRTAD FSTAQQIAER VNGAMGGPFA RAIDDMSITM DIPAQYRNNM
     VPLMASIENL DVSPDTAAKV VVDEKTGTVV LGRDVRITRT AVAHGNLQIT VQEGEQVSQP
     GPFSQGQTVV TPTTETNVRE ENRHLVIIEG ATLQELVDGL NSIGATPRDL ISILRTMQVS
     GALLAELEVI