ID A0A1N6CVU0_9SPHN Unreviewed; 373 AA.
AC A0A1N6CVU0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Flagellar P-ring protein {ECO:0000256|ARBA:ARBA00019515, ECO:0000256|HAMAP-Rule:MF_00416};
DE AltName: Full=Basal body P-ring protein {ECO:0000256|ARBA:ARBA00032344, ECO:0000256|HAMAP-Rule:MF_00416};
GN Name=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN ORFNames=SAMN02745824_1124 {ECO:0000313|EMBL:SIN62748.1};
OS Parasphingorhabdus marina DSM 22363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Parasphingorhabdus.
OX NCBI_TaxID=1123272 {ECO:0000313|EMBL:SIN62748.1, ECO:0000313|Proteomes:UP000185192};
RN [1] {ECO:0000313|Proteomes:UP000185192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22363 {ECO:0000313|Proteomes:UP000185192};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FSQW01000001; SIN62748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6CVU0; -.
DR STRING; 1123272.SAMN02745824_1124; -.
DR Proteomes; UP000185192; 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:SIN62748.1};
KW Cilium {ECO:0000313|EMBL:SIN62748.1};
KW Flagellum {ECO:0000313|EMBL:SIN62748.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185192}.
SQ SEQUENCE 373 AA; 38680 MW; 3689EEEB80763848 CRC64;
MARLFSNRII SLITIFMAAL LLFPSPAMAE RIKDLGTFQG LRANQLTGYG VVVGLPGTGD
DSLEYATLGV KGMANRFGLT LPPGINPSLK NAAAVMVTVE LPPFAKPGQR LDVTVSAIGK
AKSLRGGTLI MMPLYGADGQ VYAMAQGNLA VGGLGVGAAD GSRTTVNIPS VGRIAGGATV
ERAVDTGFNQ SPYLTFNLSE FDLTTALRVA EAINQKFPEA RAEASDGVSI RISAPASGNE
RMMMMGLIEN IEVTPADAPA RVIINARTGT VVINGAVRIS PAAISHGKLT VKVDENPTVI
QPEPFSRGQT AVEPSSEITI EEKTAPMFEL APGASLSEMV AAINAIGVTP GDLAAILDAL
KQAGALKAEL III
//
