ID   A0A1G9C849_9RHOB        Unreviewed;       367 AA.
AC   A0A1G9C849;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Flagellar P-ring protein {ECO:0000256|ARBA:ARBA00019515, ECO:0000256|HAMAP-Rule:MF_00416};
DE   AltName: Full=Basal body P-ring protein {ECO:0000256|ARBA:ARBA00032344, ECO:0000256|HAMAP-Rule:MF_00416};
DE   Flags: Precursor;
GN   Name=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN   ORFNames=SAMN04487971_101130 {ECO:0000313|EMBL:SDK47819.1};
OS   Paracoccus chinensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=525640 {ECO:0000313|EMBL:SDK47819.1, ECO:0000313|Proteomes:UP000199555};
RN   [1] {ECO:0000313|EMBL:SDK47819.1, ECO:0000313|Proteomes:UP000199555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7655 {ECO:0000313|EMBL:SDK47819.1,
RC   ECO:0000313|Proteomes:UP000199555};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNGE01000001; SDK47819.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9C849; -.
DR   STRING; 525640.SAMN04487971_101130; -.
DR   OrthoDB; 9786431at2; -.
DR   Proteomes; UP000199555; Unassembled WGS sequence.
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:SDK47819.1};
KW   Cilium {ECO:0000313|EMBL:SDK47819.1};
KW   Flagellum {ECO:0000313|EMBL:SDK47819.1};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT   CHAIN           21..367
FT                   /note="Flagellar P-ring protein"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT                   /id="PRO_5011801059"
SQ   SEQUENCE   367 AA;  38165 MW;  AA55F8F01EAC9B72 CRC64;
     MAAFTRILAL VLLLPCLAWA APVRIKDLAT VDGVRGNDLL GYGLVIGLNG TGDSLRNTPY
     TEEMLGSLLE RLGVNVTGES FRPKNVAAVM VTGTLPPFAH AGGQIDVTVS AIGDAKSLLG
     GTLIMTPLNA ADGEVYAVAQ GSIIAGGVSA EGEAASVVQG VPTSGHIPSG ARVEREVDFD
     FSQMSSFRLA LRSADFTTAA RIEKAINDDL GDGVATLLDA TTISIDSTSL GTVNPARLVG
     RIENISVEPE SRARVVVDHR SGTIVMGEEV RISRVAVSQG NLTLRVRETP MVSQPNPFSP
     GETVVVPRTD AEITQEPGIG FAEVSGESSL SDVVAGLNAL GVRPRELIDI LKAVHAAGAL
     HAEFIVN
//