ID   FLGI1_HAHCH             Reviewed;         373 AA.
AC   Q2SEX9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Flagellar P-ring protein 1 {ECO:0000255|HAMAP-Rule:MF_00416};
DE   AltName: Full=Basal body P-ring protein 1 {ECO:0000255|HAMAP-Rule:MF_00416};
DE   Flags: Precursor;
GN   Name=flgI1 {ECO:0000255|HAMAP-Rule:MF_00416}; OrderedLocusNames=HCH_04082;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(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   -!- SEQUENCE CAUTION:
CC       Sequence=ABC30795.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000155; ABC30795.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_049781229.1; NC_007645.1.
DR   AlphaFoldDB; Q2SEX9; -.
DR   SMR; Q2SEX9; -.
DR   STRING; 349521.HCH_04082; -.
DR   EnsemblBacteria; ABC30795; ABC30795; HCH_04082.
DR   KEGG; hch:HCH_04082; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; QFRPKNV; -.
DR   Proteomes; UP000000238; 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..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           25..373
FT                   /note="Flagellar P-ring protein 1"
FT                   /id="PRO_0000236302"
SQ   SEQUENCE   373 AA;  39169 MW;  983E30B35833789D CRC64;
     MRGISRLYWS LVLICFAFAP IVEASSVRLK ELARIEGVRE NSLFGYGLVV GLAGTGDTHR
     SKATLQSIAN TLQQFGISLD SDEIASRNVA AVTLTAKLPP FANSGDMIDV NVSSMGDARS
     LVGGTLLLAP LKAVNGKIYA VAQGQVSVGG FSYDLNGNVV QKNHPTVGVI PSGASVERGL
     STDLVGADGH INVILNQPDF TTASRIKNAI NKTLGPGKAR AVHAGKISVV APAGEYDLVD
     YLTRIENSVI EPDRIATVVV NERTGTVVAG GDVTIDNVTI SHGNIKVVIS TDYQVSQPVF
     VREPGRGVST VVVPDTSIDI EESVAEPVRL SSGASIADLV TALRQIKTST RDVITILQLI
     KTAGALHAQL VIQ