ID A0A369WNE4_9GAMM Unreviewed; 366 AA.
AC A0A369WNE4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 10.
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};
DE Flags: Precursor;
GN Name=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN ORFNames=DV711_07240 {ECO:0000313|EMBL:RDE23021.1};
OS Motiliproteus coralliicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Motiliproteus.
OX NCBI_TaxID=2283196 {ECO:0000313|EMBL:RDE23021.1, ECO:0000313|Proteomes:UP000253769};
RN [1] {ECO:0000313|EMBL:RDE23021.1, ECO:0000313|Proteomes:UP000253769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C34 {ECO:0000313|EMBL:RDE23021.1,
RC ECO:0000313|Proteomes:UP000253769};
RA Wang G.;
RT "Motiliproteus coralliicola sp. nov., a bacterium isolated from Coral.";
RL Submitted (JUL-2018) 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|ARBA:ARBA00008994,
CC ECO:0000256|HAMAP-Rule:MF_00416}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDE23021.1}.
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DR EMBL; QQOH01000002; RDE23021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369WNE4; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000253769; 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:RDE23021.1};
KW Cilium {ECO:0000313|EMBL:RDE23021.1};
KW Flagellum {ECO:0000313|EMBL:RDE23021.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253769};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 24..366
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5017090570"
SQ SEQUENCE 366 AA; 37855 MW; 206F1A00CC6615DA CRC64;
MKTTTRNLMI LLLGTLLSAG VQAERLKDIT DVAGVRPNQL VGYGLVVGLS GTGDKVSFTS
QTFKNMLAQF GLTLPPGTNP QSKNIAAVSI HAELPPFAKP GQLLDVTVSS IGDASSLRGG
SLLMAPLKGA DGQVYAMAQG NLVVGGLGAE GLDGSRITIN VPSVGRVPSG ATVERSVPSP
FARGDHLVLN LHTPDFTTSR RVAERINGLL GPDVATSVDA TSIRVRAPRD ASQRVTYLSV
LENLEVEPAA EVAKVIINSR TGTIIIGENV RVSPVAITHG GLTVSILENP EANQPGAFAG
GDTVVVPRSG IEVDENSGHM FSFQPGASLN EIVEAVNQVG AAPGDLMAIL EALKQSGALK
AELVVI
//
