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Database: UniProt
Entry: A0A363S4N3_9GAMM
LinkDB: A0A363S4N3_9GAMM
Original site: A0A363S4N3_9GAMM 
ID   A0A363S4N3_9GAMM        Unreviewed;       365 AA.
AC   A0A363S4N3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
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   ORFNames=DCO49_00300 {ECO:0000313|EMBL:PWB29845.1};
OS   Stenotrophomonas sp. SPM.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=2170735 {ECO:0000313|EMBL:PWB29845.1, ECO:0000313|Proteomes:UP000250746};
RN   [1] {ECO:0000313|Proteomes:UP000250746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPM {ECO:0000313|Proteomes:UP000250746};
RA   Frantz D.C., Newman J.D.;
RL   Submitted (APR-2018) 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:PWB29845.1}.
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DR   EMBL; QETL01000001; PWB29845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A363S4N3; -.
DR   Proteomes; UP000250746; 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:PWB29845.1};
KW   Cilium {ECO:0000313|EMBL:PWB29845.1};
KW   Flagellum {ECO:0000313|EMBL:PWB29845.1}.
SQ   SEQUENCE   365 AA;  38047 MW;  8B58ED35D236B6C8 CRC64;
     MALLVAIGLG ANAMAATVKV KDIARVAGVR ENQLTGYGLV FGLSGSGDSS RNRATVQSVA
     NTLRNFGVNV SDQDVASRNV AAVIVTAKLP AFAEPGQLID VQVASSGDAR SLTGGTLMLT
     PLRAADGRLY AMAQGALSVG GYQFEGMTAS LQRNHPTVGW IPSGGSIEQA SPLQMDSDGR
     SLAIVLNEPD FTNATRIAEA IRSMGEIRSA RADHAGKVSV QFDVPPDDLV ALIARLENLT
     LEQQRKARVV VNERTGTVVA GGDVRLGRVS VSHGGLKVEI RTEFKVSQPD GVYYRPGSGI
     ASVVTPSTRI DAEEGVAPLV QVPEGASVAD LISALRTARL STRDVIAVLQ SIKTAGALDG
     ELVIQ
//
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