ID   A0A1M6D5A2_9RHOB        Unreviewed;       367 AA.
AC   A0A1M6D5A2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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};
DE   Flags: Precursor;
GN   Name=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN   ORFNames=SAMN04488012_102262 {ECO:0000313|EMBL:SHI68283.1};
OS   Palleronia salina.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Palleronia.
OX   NCBI_TaxID=313368 {ECO:0000313|EMBL:SHI68283.1, ECO:0000313|Proteomes:UP000184040};
RN   [1] {ECO:0000313|EMBL:SHI68283.1, ECO:0000313|Proteomes:UP000184040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26892 {ECO:0000313|EMBL:SHI68283.1,
RC   ECO:0000313|Proteomes:UP000184040};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
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; FQZA01000002; SHI68283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6D5A2; -.
DR   STRING; 313368.SAMN04488012_102262; -.
DR   Proteomes; UP000184040; 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:SHI68283.1};
KW   Cilium {ECO:0000313|EMBL:SHI68283.1};
KW   Flagellum {ECO:0000313|EMBL:SHI68283.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184040};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT   CHAIN           21..367
FT                   /note="Flagellar P-ring protein"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT                   /id="PRO_5013409540"
SQ   SEQUENCE   367 AA;  37816 MW;  69637AEE9711AA79 CRC64;
     MRRLWLTCAV LILGLTAASA SPVRIKDLVE FDGVRGNDLL GYGLVVGLNG TGDGLRNSPF
     TEEIMASMLE RLGVNVTGEQ FRPNNVAAVL VTAVLPPFAR AGSQIDVTVS AIGDASSLLG
     GTLVMTPLNA ADGQIYAVAQ GTIIAGGATA EGDAATVTQG VPTAGAVPAG ARVEREIDFD
     FGSLTSVRLA LRTPDFTTAA RIEQAINADL NRGVAIMLDA GTVEVDIAAT RARSPAHALG
     RIENIRVEPE RRARVVVDQR SGTIVMGSDV RISQVAVSQG GLTIRVEEAP VAVQPNPFAP
     GETVVVPRTN VGIEDEAGIG LAVVPDGTSL SEVVAGLNAL GVAPRDMIDI LKAIKSAGAL
     HAELVVQ
//