ID A0A432WPX6_9GAMM Unreviewed; 368 AA.
AC A0A432WPX6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 10.
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=CWE11_03510 {ECO:0000313|EMBL:RUO35833.1};
OS Aliidiomarina sanyensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Aliidiomarina.
OX NCBI_TaxID=1249555 {ECO:0000313|EMBL:RUO35833.1, ECO:0000313|Proteomes:UP000288405};
RN [1] {ECO:0000313|EMBL:RUO35833.1, ECO:0000313|Proteomes:UP000288405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GYP-17 {ECO:0000313|EMBL:RUO35833.1,
RC ECO:0000313|Proteomes:UP000288405};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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:RUO35833.1}.
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DR EMBL; PIPM01000002; RUO35833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432WPX6; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000288405; 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:RUO35833.1};
KW Cilium {ECO:0000313|EMBL:RUO35833.1};
KW Flagellum {ECO:0000313|EMBL:RUO35833.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000288405}.
SQ SEQUENCE 368 AA; 39178 MW; 6D29F54322143653 CRC64;
MKRLFYIGLL AFGLLVQGPV HAERLKDLAD FAGVRDNVLV GYGLVVGLDG TGDQTTQAPF
TGQSLTNMLS QLGVTVPPGT NMQLRNVAAV MVTADLPPFS RQGQRLDVTV SSVGNARSLR
GGTLLMTPLR GADGEIYALA QGNLLIAGAT AEAAGSRETI NHQSAGRISR GAIVEREVPL
NMNAQGNGEL ELHLRSADFS TAERVVTRIN EEFGNFVASA VDGRTIRLFG PQDENERVRF
MARVENLRVT PDEGRARVVL NSRTGSVVLN GNVRLHQAAV AHGNLAVSID TRRGVSQPRA
FSPGQTVIVE EADIQLTQDD GVLNVVEGVD LMEVVNALNA LGATPMDLMA ILEALKASGS
LRAELEII
//
