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Database: UniProt
Entry: A0A410GGK9_9BURK
LinkDB: A0A410GGK9_9BURK
Original site: A0A410GGK9_9BURK 
ID   A0A410GGK9_9BURK        Unreviewed;       355 AA.
AC   A0A410GGK9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Flagellar P-ring protein {ECO:0000256|HAMAP-Rule:MF_00416};
DE   AltName: Full=Basal body P-ring protein {ECO:0000256|HAMAP-Rule:MF_00416};
GN   Name=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN   ORFNames=CKA81_03045 {ECO:0000313|EMBL:QAA95437.1};
OS   Pollutimonas thiosulfatoxidans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pollutimonas.
OX   NCBI_TaxID=2028345 {ECO:0000313|EMBL:QAA95437.1, ECO:0000313|Proteomes:UP000283474};
RN   [1] {ECO:0000313|EMBL:QAA95437.1, ECO:0000313|Proteomes:UP000283474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ye3 {ECO:0000313|Proteomes:UP000283474};
RA   Park S.-J., Kim H.;
RL   Submitted (AUG-2017) 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:0000256|ARBA:ARBA00002591, ECO:0000256|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:0000256|HAMAP-Rule:MF_00416}.
CC   -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC       {ECO:0000256|ARBA:ARBA00004117, ECO:0000256|HAMAP-Rule:MF_00416}.
CC   -!- SIMILARITY: Belongs to the FlgI family. {ECO:0000256|HAMAP-
CC       Rule:MF_00416}.
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DR   EMBL; CP022987; QAA95437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A410GGK9; -.
DR   KEGG; pus:CKA81_03045; -.
DR   OrthoDB; 9786431at2; -.
DR   Proteomes; UP000283474; 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; FLAGELLAR P-RING PERIPLASMIC PROTEIN FLGI; 1.
DR   PANTHER; PTHR30381:SF0; FLAGELLAR P-RING PROTEIN; 1.
DR   Pfam; PF02119; FlgI; 1.
DR   PRINTS; PR01010; FLGPRINGFLGI.
PE   3: Inferred from homology;
KW   Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143, ECO:0000256|HAMAP-
KW   Rule:MF_00416}; Cell projection {ECO:0000313|EMBL:QAA95437.1};
KW   Cilium {ECO:0000313|EMBL:QAA95437.1};
KW   Flagellum {ECO:0000313|EMBL:QAA95437.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283474}.
SQ   SEQUENCE   355 AA;  36669 MW;  056C1851D38D7A4E CRC64;
     MMAPLALQAE RVKDLASIQG VRANQLIGYG LVVGLDGSGD QVRQTPFTQQ SLTNMLSQLG
     ITVPQGTNMQ VKNVAAVMVT ARLPAFARPG QTVDVVVSSM GNAKSLRGGT LLMTPLKGAN
     GQVYAMAQGN LLVGGAGAQA GGSSVQVNQL NGGIISNGAI IERSVPTIYA QDGIINLELN
     TTDFGTAQNM VAALNQQFGS GIATALDGRV IQVRGPAAPD AQAAFLSQVE NLQVRVAPAR
     AKVVINARTG SVVMNRTVTI DEAAIAYGNL SVVISQESQV NQPDTPFGGG QTVVTENTQI
     EMRSDAGSLQ RVTTSANLAD VVNALNALGA TPQDLLSILQ NLKSAGALRA DLEII
//
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