ID I9P5X9_9ALTE Unreviewed; 364 AA.
AC I9P5X9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
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 ECO:0000313|EMBL:EIW90249.1};
GN ORFNames=AGRI_00220 {ECO:0000313|EMBL:EIW90249.1};
OS Alishewanella agri BL06.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alishewanella.
OX NCBI_TaxID=1195246 {ECO:0000313|EMBL:EIW90249.1, ECO:0000313|Proteomes:UP000035062};
RN [1] {ECO:0000313|EMBL:EIW90249.1, ECO:0000313|Proteomes:UP000035062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL06 {ECO:0000313|EMBL:EIW90249.1,
RC ECO:0000313|Proteomes:UP000035062};
RX PubMed=22933763; DOI=10.1128/JB.01129-12;
RA Kim J., Jung J., Sung J.S., Chun J., Park W.;
RT "Genome Sequence of Pectin-Degrading Alishewanella agri, Isolated from
RT Landfill Soil.";
RL J. Bacteriol. 194:5135-5136(2012).
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:EIW90249.1}.
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DR EMBL; AKKU01000001; EIW90249.1; -; Genomic_DNA.
DR RefSeq; WP_008983027.1; NZ_AKKU01000001.1.
DR AlphaFoldDB; I9P5X9; -.
DR STRING; 1195246.AGRI_00220; -.
DR PATRIC; fig|1195246.3.peg.44; -.
DR eggNOG; COG1706; Bacteria.
DR Proteomes; UP000035062; 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:EIW90249.1};
KW Cilium {ECO:0000313|EMBL:EIW90249.1};
KW Flagellum {ECO:0000313|EMBL:EIW90249.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035062};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 22..364
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5009014964"
SQ SEQUENCE 364 AA; 38216 MW; 78350A3FDB06E4DE CRC64;
MRSRFLLVGL LLALISVTAD AARIKDVADI EGVRSNQLVG YGLVVGLPGT GEQSPFTEQS
FRTMLANFGI NLPAGTRTQI KNVAAVAIHA ELPAFAKPGQ TIDITVSSVG SAKSLRGGTL
LQTFLTGLDG NVYAVAQGSL IVSGLGAEGL DGSRILVNTP TVGRIPNGAV VEREVESPFA
KGDFITFNLK RPDFTTAKRL AETINGFMGP ETAFSLDASS VQVRAPRDIS QRVSYLSTLE
NLTFQPADQS AKIIINSRTG TIVIGKDVRL FPAAVTHGGL TVTIEENPQV SQPNPLAGGD
TAIVQDSIIN VSPENSRMFK FDPGVTLDDL VRTVNAVGAA PGDLMAILEA LKEAGAIHGE
LVVI
//
