ID A0A1I4R4U6_9PSED Unreviewed; 367 AA.
AC A0A1I4R4U6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN04487858_103142 {ECO:0000313|EMBL:SFM47269.1};
OS Pseudomonas sp. ok602.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1761898 {ECO:0000313|EMBL:SFM47269.1, ECO:0000313|Proteomes:UP000199362};
RN [1] {ECO:0000313|Proteomes:UP000199362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK602 {ECO:0000313|Proteomes:UP000199362};
RA Varghese N., Submissions S.;
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|ARBA:ARBA00008994,
CC ECO:0000256|HAMAP-Rule:MF_00416}.
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DR EMBL; FOUL01000003; SFM47269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4R4U6; -.
DR STRING; 1761898.SAMN04487858_103142; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000199362; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143, ECO:0000256|HAMAP-
KW Rule:MF_00416}; Cell projection {ECO:0000313|EMBL:SFM47269.1};
KW Cilium {ECO:0000313|EMBL:SFM47269.1};
KW Flagellum {ECO:0000313|EMBL:SFM47269.1};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 23..367
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5011801725"
SQ SEQUENCE 367 AA; 37907 MW; 993CF84B08B4C561 CRC64;
MRRFFNVLCA GALVACTLPA GAVPMLDLVD IEGIRGNQLI GYGLVVGLDG SGDKNQVKFT
NQSVVNMIKQ FGVNLPPNMD PKLKNVAAVS VTATMPTSYS AGQTVDVVVS SLGDAKSLRG
GQLLLTPLLG VDGETYALAQ GALVVGGLNA QGSSGSSVAI NTANGGRIPN GATVERMIPS
DFLTRDDVML NLRTPSFQTA SRVVDAVNAR FGSGTATALN ATKVSLRAPV SSNQRISFLA
MLEAVEVVEG RTRPKVVFNS RTGTVVVGQG VRVKAAAVAH GTLTVTISEN PQVSQPGAFS
GGQTAVVPRS DVNVSQEANA MFKWPEGASL ESIINTVNSL GATPDDVMSI LQSLEQAGAL
SAELIVI
//
