ID A0A0X8GPL2_9BURK Unreviewed; 360 AA.
AC A0A0X8GPL2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=VN23_16590 {ECO:0000313|EMBL:AMC36096.1};
OS Janthinobacterium sp. B9-8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC36096.1, ECO:0000313|Proteomes:UP000069577};
RN [1] {ECO:0000313|EMBL:AMC36096.1, ECO:0000313|Proteomes:UP000069577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B9-8 {ECO:0000313|EMBL:AMC36096.1,
RC ECO:0000313|Proteomes:UP000069577};
RA Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT isolated from low temperature sewage.";
RL Submitted (JAN-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; CP014222; AMC36096.1; -; Genomic_DNA.
DR RefSeq; WP_046353575.1; NZ_CP014222.1.
DR AlphaFoldDB; A0A0X8GPL2; -.
DR STRING; 1236179.VN23_16590; -.
DR KEGG; jab:VN23_16590; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000069577; 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:AMC36096.1};
KW Cilium {ECO:0000313|EMBL:AMC36096.1};
KW Flagellum {ECO:0000313|EMBL:AMC36096.1};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 19..360
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5008998143"
SQ SEQUENCE 360 AA; 37611 MW; D8F2631606F22F8E CRC64;
MKFKCLFWLC LLLQTASAQE LRTLVNVEGI RENQLMGYGV VVGLNGTGDN SQVKFAGQSV
ANLLRQFGIK QTGETKVKNV AGVVVNAVLP SGYHKGQTID ITVSSLGDAK SLRGGVLLLT
PLRAADGEVY ALAQGNVVIT GLSAQGSSGS SVTVNTPTSG RIPNGASVER EIESDFDTRP
TVTLSLKRPS FQNATQIVSA VNQRFGKIAS TKNATNIEII APSDPSERVA FVARLEALNI
TAAAEVPRVV FNSRTGTVVI SQGVTVRAAA VSHGSLRIVI SEAPAVSQPG AFSNGTTATV
PRSKVDVREG SGQMFRWPPG ASLKTIIDTI NSTGASPDDI MAILQALDQA GALDGELVVI
//
