ID A0A3N1XJZ2_9BURK Unreviewed; 384 AA.
AC A0A3N1XJZ2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=EC845_1084 {ECO:0000313|EMBL:ROR25047.1};
OS Comamonas sp. BIGb0124.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=2485130 {ECO:0000313|EMBL:ROR25047.1, ECO:0000313|Proteomes:UP000267274};
RN [1] {ECO:0000313|EMBL:ROR25047.1, ECO:0000313|Proteomes:UP000267274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIGb0124 {ECO:0000313|EMBL:ROR25047.1,
RC ECO:0000313|Proteomes:UP000267274};
RA Samuel B.;
RT "Genomic analyses of the natural microbiome of Caenorhabditis elegans.";
RL Submitted (NOV-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|HAMAP-
CC 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:ROR25047.1}.
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DR EMBL; RJVF01000008; ROR25047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1XJZ2; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000267274; 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:ROR25047.1};
KW Cilium {ECO:0000313|EMBL:ROR25047.1};
KW Flagellum {ECO:0000313|EMBL:ROR25047.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000267274};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 38..384
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5018344577"
SQ SEQUENCE 384 AA; 38923 MW; 470FF4793E1B727C CRC64;
MRPNALSIPR SASARHLPAV ALLAATVLMA AVMPAHALRV KEVASVQGVR TNQLTGYGLV
VGLDGTGDQA TQVPFTTQSL ANYLQQMGIT VPASAQSRMQ PKNVAAVIVT AQLPAFAQPG
QTIDINVSSM GNAKSLRGGT LIMTPLRGAD GDIYALAQGN VVVGGAGASA NGSKVQINQL
SGGRIPAGGQ VERAVATGLQ QGDTVTLNLN SVDFSTAQLV VQAINGRLGD GLAQAIDGRT
IEVAAPAAPS DRVAFIARIE ELALTVPTPA AKVVINSRTG SIVLNQAVTL GACAVAHGSL
SIVISTTPVI SQPGAFSGGQ TVVTQQSEIS VAQTPSALVQ LPASPQLTDV VRALNTLGAN
PQDLISILQA IKSAGALNAE LEII
//
