ID A0A0W0VYE6_9GAMM Unreviewed; 368 AA.
AC A0A0W0VYE6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=Lisr_1290 {ECO:0000313|EMBL:KTD24994.1};
OS Legionella israelensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=454 {ECO:0000313|EMBL:KTD24994.1, ECO:0000313|Proteomes:UP000054761};
RN [1] {ECO:0000313|EMBL:KTD24994.1, ECO:0000313|Proteomes:UP000054761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD24994.1,
RC ECO:0000313|Proteomes:UP000054761};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD24994.1}.
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DR EMBL; LNYH01000064; KTD24994.1; -; Genomic_DNA.
DR RefSeq; WP_058501648.1; NZ_UGOE01000001.1.
DR AlphaFoldDB; A0A0W0VYE6; -.
DR STRING; 454.Lisr_1290; -.
DR PATRIC; fig|454.4.peg.1396; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000054761; 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:KTD24994.1};
KW Cilium {ECO:0000313|EMBL:KTD24994.1};
KW Flagellum {ECO:0000313|EMBL:KTD24994.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054761};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 20..368
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5022282692"
SQ SEQUENCE 368 AA; 39705 MW; 439BB626FC096B89 CRC64;
MFKCCLPFVF LLLFFPLHAE VRLKSLTHIS GLQENTLTGY GLVIGLAGSG DSRRNKDTTQ
AIANLLQSFG VNLSPSEINS RNSATVIVTT KLPPLVHQGD KIDVNVSSLG DARSLLGGTL
LVTPLKGADD QIYALAQGPI SIGGFKYDLF GNVIQKNHPT TGMIPGGAVV EKSLYTDLTD
KSGIFHLILN RPDFTTADLI EVSINQKFGI NTALARSAQD IEIHPPQQYS KRLIRFISQL
ENIVLTPDNI PTIVVNERTG VVIAGADVKL DAVTISHGNL HIAISTEYNV SQPTLIRNVG
PQVHTSITPS TNIQVRESNA NTVQLKKEAT VADLIAALNK VKTSTRDIIS ILESLQRAGA
LHAELIIQ
//
