ID A0A2A2F6T2_9GAMM Unreviewed; 364 AA.
AC A0A2A2F6T2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=CK501_07870 {ECO:0000313|EMBL:PAU80359.1};
OS Halovibrio salipaludis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halovibrio.
OX NCBI_TaxID=2032626 {ECO:0000313|EMBL:PAU80359.1, ECO:0000313|Proteomes:UP000218896};
RN [1] {ECO:0000313|EMBL:PAU80359.1, ECO:0000313|Proteomes:UP000218896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL5-2 {ECO:0000313|EMBL:PAU80359.1,
RC ECO:0000313|Proteomes:UP000218896};
RA Dong X., Zhang G.;
RT "Halovibrio sewagensis sp. nov., isolated from wastewater of high
RT salinity.";
RL Submitted (AUG-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:PAU80359.1}.
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DR EMBL; NSKD01000003; PAU80359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2F6T2; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000218896; 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:PAU80359.1};
KW Cilium {ECO:0000313|EMBL:PAU80359.1};
KW Flagellum {ECO:0000313|EMBL:PAU80359.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218896};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 22..364
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5013411902"
SQ SEQUENCE 364 AA; 37649 MW; 47FB53E48155933A CRC64;
MLNRIAAVLV LVALVAGPVQ ADRLKDLTSV KGVRDNQLVG YGLVVGLDGS GDGAPFTNQS
LRNMMDQFGI TIPPGVDPGA DNVAAVMVTA DLQPFASPGQ EIDVTVSSVG DADSLRGGTL
LMTPLQGADG QTYAMAQGSL VVGGFGAEGQ DGSSISVNVP SVGRIPQGAT VERQVPTAFS
EGDTITLNLR NPDFTTARRV VEAINNKLGS ETAYAKDASS VRVRAPRDAS QRVSFLSILE
NIEITPAEES AKVVINSRTG TIVVGENVKV SPAAVTHGNL SVTITENPEA VAPGLFGDGD
PLVVPQTDVA IEQEEARMFK FGPAVTLNEI VQSVNQVGAA PGDIMAVLEA LKQAGALRAE
LIVI
//
