ID A0A254QZS2_9RHOB Unreviewed; 369 AA.
AC A0A254QZS2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
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 ECO:0000313|EMBL:OWU83195.1};
GN ORFNames=ATO6_20355 {ECO:0000313|EMBL:OWU83195.1};
OS Oceanicola sp. 22II-s10i.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceanicola.
OX NCBI_TaxID=1317116 {ECO:0000313|EMBL:OWU83195.1, ECO:0000313|Proteomes:UP000197567};
RN [1] {ECO:0000313|EMBL:OWU83195.1, ECO:0000313|Proteomes:UP000197567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s10i {ECO:0000313|EMBL:OWU83195.1,
RC ECO:0000313|Proteomes:UP000197567};
RA Lai Q., Li G., Shao Z.;
RT "Oceanicola sp. 22II-s10i Genome Sequencing.";
RL Submitted (APR-2013) 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:OWU83195.1}.
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DR EMBL; AQQU01000010; OWU83195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254QZS2; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000197567; 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:OWU83195.1};
KW Cilium {ECO:0000313|EMBL:OWU83195.1};
KW Flagellum {ECO:0000313|EMBL:OWU83195.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000197567};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 22..369
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5013408979"
SQ SEQUENCE 369 AA; 38195 MW; 54F021FAFDDCA901 CRC64;
MKKSRRTLAG LIALAALGWQ AAVADVRIKD IVSVEGVREN QLVGYGLVVG LNGTGDGLRN
SPFTEKSIQG MLERLGVGNL SEDQIKTRNT AAVMVTAMLP PFARRGSTID VVVSSLGDAS
SLRGGTLIVT PLTGADGEVY AVAQGPIAVA GFAAQGINAS IVEGVPTVAR IENGATVENE
VDFSLASLKS IRLNLRNPDF TTALRVEEAI NAALGGGTAR ALDPATIEIQ TPDKAATPGL
LAQVENLRVQ PDNIARVVID ARSGTIVIGA DVRIDRVAVS QGGLTVMIRE DPQVSQPNPI
TIGGTTVVVP STTVGVDKKE AHFTILEGDV SLQRLVDGLN AIGLGATETI SILQAIKAAG
ALHADLEII
//
