ID L0GZH5_9GAMM Unreviewed; 393 AA.
AC L0GZH5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=Thimo_3495 {ECO:0000313|EMBL:AGA92158.1};
OS Thioflavicoccus mobilis 8321.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thioflavicoccus.
OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA92158.1, ECO:0000313|Proteomes:UP000010816};
RN [1] {ECO:0000313|EMBL:AGA92158.1, ECO:0000313|Proteomes:UP000010816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8321 {ECO:0000313|EMBL:AGA92158.1,
RC ECO:0000313|Proteomes:UP000010816};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL Submitted (SEP-2011) 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}.
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DR EMBL; CP003051; AGA92158.1; -; Genomic_DNA.
DR AlphaFoldDB; L0GZH5; -.
DR STRING; 765912.Thimo_3495; -.
DR KEGG; tmb:Thimo_3495; -.
DR PATRIC; fig|765912.4.peg.3427; -.
DR eggNOG; COG1706; Bacteria.
DR HOGENOM; CLU_045235_1_0_6; -.
DR Proteomes; UP000010816; 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:AGA92158.1};
KW Cilium {ECO:0000313|EMBL:AGA92158.1};
KW Flagellum {ECO:0000313|EMBL:AGA92158.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010816};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 31..393
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5009016621"
SQ SEQUENCE 393 AA; 40659 MW; 464CF1CC7A79432F CRC64;
MRMPFPAHSA GHWVRWFLIG CLLSPLVAVA GAYGDSDPAG DPVANGWGTR IKDIASVAGV
RSNQLVGYGL VVGLNGTGDK TNTTQFTAQS VQNMLRQLGV AIPADARIRP ENVAAVLVTA
TLPPFAKQGQ TIDVTVSSIG NAESVRGGVL LMTPLKAGDG QIYALAQGNL VVGGFGARGA
DGSKITVNHP SAGRIPNGAT VERAVAGPFA DGGDLVLQFQ DPDFTTAQRV ADAINQRLGP
GQAEPLDAAS VRVLAPDDVG ERVGFVALIE NLRVEPADAP ARVIINSRTG TVVIGQHVVV
LPAAVSHGNL IVTISENPVV SQPAPFSDGV TVMGSDSQIE IQQEDRMFLL KPGISLEEIV
QAVNRVGAAP GDLVAILEAL RKAGALRASL EVI
//
