ID Q1MQC9_LAWIP Unreviewed; 379 AA.
AC Q1MQC9;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 ECO:0000313|EMBL:CAJ54798.1};
GN OrderedLocusNames=LI0744 {ECO:0000313|EMBL:CAJ54798.1};
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54798.1, ECO:0000313|Proteomes:UP000002430};
RN [1] {ECO:0000313|EMBL:CAJ54798.1, ECO:0000313|Proteomes:UP000002430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54798.1,
RC ECO:0000313|Proteomes:UP000002430};
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) 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}.
CC -!- SIMILARITY: Belongs to the FlgI family. {ECO:0000256|HAMAP-
CC Rule:MF_00416}.
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DR EMBL; AM180252; CAJ54798.1; -; Genomic_DNA.
DR RefSeq; WP_011526827.1; NC_008011.1.
DR AlphaFoldDB; Q1MQC9; -.
DR STRING; 363253.LI0744; -.
DR KEGG; lip:LI0744; -.
DR eggNOG; COG1706; Bacteria.
DR HOGENOM; CLU_045235_1_0_7; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000002430; Chromosome.
DR GO; GO:0009428; C:bacterial-type flagellum basal body, distal rod, P ring; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:CAJ54798.1};
KW Cilium {ECO:0000313|EMBL:CAJ54798.1};
KW Flagellum {ECO:0000313|EMBL:CAJ54798.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002430};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 379 AA; 39928 MW; C8BAFDD8592A2A17 CRC64;
MLSSIIRPTK NCLLHFIIRS SYLTLLFIAV FHNPAQSVRI KDIATFSGVR NNQLIGYGLV
IGLAGTGDKR DSPFTASSMT NMLERMGVAV DANKIKPKNV AAVMVTANMP VSARPGTELD
VTVSSVGDAK SLQGGVLLQT PLKGVDGKVY ALAQGSLIIG GYSAEGTAAS VQKNSTTVGS
IPGGGIVEKG IPFDFNTQQN LTLNMNSNDF STTMQVVNRL NATMGGNFAS AIDAGTVRID
IPPAYKGNLV PLIASIENLE INPESVAKVV VDEKTGTIVL GREVRLSRVA VAHGNLQVVI
QESAQVSQPG PFSQGQTVIT PETNLTLQEE TKRLNLLEGA SLQELVDGLN AIGATPRDMI
SILRALKAAG SLHAQLEVL
//
