ID   FLGI_OLEA2              Reviewed;         370 AA.
AC   Q30WJ7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=Dde_3155;
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21685289; DOI=10.1128/jb.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(2011).
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; CP000112; ABB39949.1; -; Genomic_DNA.
DR   RefSeq; WP_011368903.1; NC_007519.1.
DR   AlphaFoldDB; Q30WJ7; -.
DR   SMR; Q30WJ7; -.
DR   STRING; 207559.Dde_3155; -.
DR   EnsemblBacteria; ABB39949; ABB39949; Dde_3155.
DR   KEGG; dde:Dde_3155; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_7; -.
DR   OMA; KTIQITR; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000002710; 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..28
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           29..370
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000236300"
SQ   SEQUENCE   370 AA;  39066 MW;  1073E3AC01DFF2A1 CRC64;
     MTFFTRCFRR GALLFLLAVL LLPSPAQAVR IKDIASFGGV RDNDLMGYGL VVGLGGTGDK
     KSSTFTISSM VNMLDKMGIA VDRTKLTPKN VAAVMVTTRM PVSARPGSRL DITVSSLGDA
     TSLLGGVLLM TPMKGVDGKV YALAQGPLAL GGFSAEGDAA RAQKNITTVG RIPGGAVVER
     AVPFEFNTQN KLTLHMNVQD FSTTMQVVDR LNDNMGGQFA SARDIATVDI MVPPAYRGNL
     VPLMASLENL PVTPDSPARV VVDEKTGTVV VGNSVRISKV AVSHGNLQIV VQENPQVSQP
     GAFSPGQTVV TPQTDIAAQE ENRRLVMMEG ATLQELVDGL NSIGATPRDL ISILRTLKAA
     GALHAELEVI