ID A0A1Y1R5Y6_9GAMM Unreviewed; 370 AA.
AC A0A1Y1R5Y6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=B0D91_06030 {ECO:0000313|EMBL:OQX37830.1};
OS Oceanospirillales bacterium LUC14_002_19_P2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales.
OX NCBI_TaxID=1940822 {ECO:0000313|EMBL:OQX37830.1, ECO:0000313|Proteomes:UP000192421};
RN [1] {ECO:0000313|EMBL:OQX37830.1, ECO:0000313|Proteomes:UP000192421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LUC14_002_19_P2 {ECO:0000313|EMBL:OQX37830.1};
RA Lim S.J., Davis B.G., Gill D.E., Engel A.S., Anderson L.C., Campbell B.J.;
RT "Novel co-symbiosis in the unique lucinid bivalve Phacoides pectinatus.";
RL Submitted (FEB-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|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:OQX37830.1}.
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DR EMBL; MUIA01000168; OQX37830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1R5Y6; -.
DR Proteomes; UP000192421; 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:OQX37830.1};
KW Cilium {ECO:0000313|EMBL:OQX37830.1};
KW Flagellum {ECO:0000313|EMBL:OQX37830.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192421}.
SQ SEQUENCE 370 AA; 38716 MW; 281B471E67392552 CRC64;
MGKDACKRQI AFFMGLLLFL IAVPARAERL LDLVDIQGVR NNPLIGYGLI VGLNGTGDKS
TEFTDQSLKN LLREFGVTQA GTDLKSKNVA AVSVHATLTP FVRAGQRIDI SVSSLGDAKS
LSGGTLLMTP LKGIDGEIYA VAQGDLVVGG AGASGASGSS VTINTLTVGR IPNGAIVERS
VPSSFSSNRE IVLNLRDPGF STARRIVQAV NQKFGPDVAR ARDSASIVIA APRDSSQRVT
FMSVLENLDI EAAAPPARVI FNSRTGTVVI GQHVRVLPAA VSHGSLIVTI NEGTKVSQPE
AESLGQTVVT PESEVTIEQQ RGALFMLPEE ASLQDIISAI NSVGASPADL MSILQALKQA
GALRAELIVI
//
