GenomeNet

Database: UniProt
Entry: A0A1I4CTW7_9PROT
LinkDB: A0A1I4CTW7_9PROT
Original site: A0A1I4CTW7_9PROT 
ID   A0A1I4CTW7_9PROT        Unreviewed;       367 AA.
AC   A0A1I4CTW7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=SAMN05216302_101732 {ECO:0000313|EMBL:SFK84060.1};
OS   Nitrosomonas aestuarii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=52441 {ECO:0000313|EMBL:SFK84060.1, ECO:0000313|Proteomes:UP000199533};
RN   [1] {ECO:0000313|Proteomes:UP000199533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm69 {ECO:0000313|Proteomes:UP000199533};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOSP01000017; SFK84060.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4CTW7; -.
DR   STRING; 52441.SAMN05216302_101732; -.
DR   OrthoDB; 9786431at2; -.
DR   Proteomes; UP000199533; 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:SFK84060.1};
KW   Cilium {ECO:0000313|EMBL:SFK84060.1};
KW   Flagellum {ECO:0000313|EMBL:SFK84060.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199533};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT   CHAIN           23..367
FT                   /note="Flagellar P-ring protein"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT                   /id="PRO_5011802622"
SQ   SEQUENCE   367 AA;  38200 MW;  03B64B43FFDC45FA CRC64;
     MIRIKVIFIV AFLLLSPCTS QAERIKDLAS IQGVRNNQLI GYGLVVGLDG SGDQTTQTPF
     TVQSIINMLG QLGVNLPPGT NLQLRNVAAV MVTATLPAFA RPGQMIDVTV SSMGNAKSLR
     GGTLLMTPLK GADNQVYAMA QGNILVGGAG AAAAGSSVQV NHLNAGRISG GATVERAVPS
     ALGQAEYINL ELNTTNFTNV KLIVNAINGF YPNAAAAIDG RSVQVRAPID NNQRVMFISQ
     IESLEITPAR DAAKVIVNSR TGSVAMNQAV TLESSAIAHG NLSIIINNEP VISQPGPFAE
     RGETVVAQRA QVEIRSDEGN LMLLSGGADL GEVVKALTAI GATTQDLLSI LQALKAAGSL
     RAELEII
//
DBGET integrated database retrieval system